HIV molecular immunology database

 

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Found 44 matching records:

Displaying record number 17

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MAb ID 12G-A8g2
HXB2 Location Gag(86-115)
DNA(1045..1134)
Gag Epitope Map
Author Location p17(86-115)
Epitope YCVHQRIEIKDTKEALDKIEEEQNKSKKKA Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

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References

Showing 2 of 2 references.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Shang1991 F. Shang, H. Huang, K. Revesz, H.-C. Chen, R. Herz, and A. Pinter. Characterization of monoclonal antibodies against the human immunodeficiency virus matrix protein, p17gag: identification of epitopes exposed at the surfaces of infected cells. J. Virol., 65:4798-4804, 1991. Six MAbs with linear epitopes were mapped. These Abs could only bind to HIV-infected cells that had been permeablized with acetone. Only G11g1 and G11h3, two antibodies that did not bind to peptides, but only to intact p17, could react with live HIV-1 infected cells. These antibodies were not neutralizing. PubMed ID: 1714518. Show all entries for this paper.


Displaying record number 19

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MAb ID 12I-D12g2
HXB2 Location Gag(86-115)
DNA(1045..1134)
Gag Epitope Map
Author Location p17(86-115)
Epitope YCVHQRIEIKDTKEALDKIEEEQNKSKKKA Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Shang1991 F. Shang, H. Huang, K. Revesz, H.-C. Chen, R. Herz, and A. Pinter. Characterization of monoclonal antibodies against the human immunodeficiency virus matrix protein, p17gag: identification of epitopes exposed at the surfaces of infected cells. J. Virol., 65:4798-4804, 1991. Six MAbs with linear epitopes were mapped. These Abs could only bind to HIV-infected cells that had been permeablized with acetone. Only G11g1 and G11h3, two antibodies that did not bind to peptides, but only to intact p17, could react with live HIV-1 infected cells. These antibodies were not neutralizing. PubMed ID: 1714518. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 20

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MAb ID 12G-H1c7
HXB2 Location Gag(86-115)
DNA(1045..1134)
Gag Epitope Map
Author Location p17(86-115)
Epitope YCVHQRIEIKDTKEALDKIEEEQNKSKKKA Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) rat(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Shang1991 F. Shang, H. Huang, K. Revesz, H.-C. Chen, R. Herz, and A. Pinter. Characterization of monoclonal antibodies against the human immunodeficiency virus matrix protein, p17gag: identification of epitopes exposed at the surfaces of infected cells. J. Virol., 65:4798-4804, 1991. Six MAbs with linear epitopes were mapped. These Abs could only bind to HIV-infected cells that had been permeablized with acetone. Only G11g1 and G11h3, two antibodies that did not bind to peptides, but only to intact p17, could react with live HIV-1 infected cells. These antibodies were not neutralizing. PubMed ID: 1714518. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 18

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MAb ID 12G-D7h11
HXB2 Location Gag(86-115)
DNA(1045..1134)
Gag Epitope Map
Author Location p17(86-115)
Epitope YCVHQRIEIKDTKEALDKIEEEQNKSKKKA Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Shang1991 F. Shang, H. Huang, K. Revesz, H.-C. Chen, R. Herz, and A. Pinter. Characterization of monoclonal antibodies against the human immunodeficiency virus matrix protein, p17gag: identification of epitopes exposed at the surfaces of infected cells. J. Virol., 65:4798-4804, 1991. Six MAbs with linear epitopes were mapped. These Abs could only bind to HIV-infected cells that had been permeablized with acetone. Only G11g1 and G11h3, two antibodies that did not bind to peptides, but only to intact p17, could react with live HIV-1 infected cells. These antibodies were not neutralizing. PubMed ID: 1714518. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 24

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MAb ID 11H9
HXB2 Location Gag(101-115)
DNA(1090..1134)
Gag Epitope Map
Author Location p17(101-115 SF2)
Research Contact R. B. Ferns and R. S. Tedder
Epitope LEKIEEEQNKSKKKA? Epitope Alignment
LEKIEEEQNKSKKKA? epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type inactivated HIV
Vaccine strain B clade CBL-1
Vaccine component HIV-1

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Ferns1987 R. B. Ferns, R. S. Tedder, and R. A. Weiss. Characterization of Monoclonal Antibodies against the Human Immunodeficiency Virus gag Products and Their Use in Monitoring HIV Isolate Variation. J. Gen. Virol., 68:1543-1551, 1987. PubMed ID: 2438375. Show all entries for this paper.

Ferns1989 R. B. Ferns, J. C. Partridge, R. P. Spence, N. Hunt, and R. S. Tedder. Epitope Location of 13 Anti-Gag HIV-1 Monoclonal Antibodies Using Oligopeptides and their Cross-Reactivity with HIV-2. AIDS, 3:829-834, 1989. PubMed ID: 2483619. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 943

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MAb ID anti-K159
HXB2 Location Pol(866-878)
DNA(4680..4718)
Pol Epitope Map
Author Location Integrase(163-175)
Epitope VESMNKELKKIIG Epitope Alignment
VESMNKELKKIIG epitope logo
Ab Type  
Neutralizing  
Species (Isotype) rabbit(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine component Int

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Maroun1999 R. G. Maroun, D. Krebs, M. Roshani, H. Porumb, C. Auclair, F. Troalen, and S. Fermandjian. Conformational Aspects of HIV-1 Integrase Inhibition by a Peptide Derived from the Enzyme Central Domain and by Antibodies Raised against This Peptide. Eur. J. Biochem., 260:145-155, 1999. PubMed ID: 10091594. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 243

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MAb ID 10.1
HXB2 Location Rev(33-48)
DNA(8399..8446)
Rev Epitope Map
Author Location Rev(33-48)
Epitope GTRQARRNRRRRWRER? Epitope Alignment
GTRQARRNRRRRWRER? epitope logo
Ab Type  
Neutralizing  
Species (Isotype)  
Patient  
Immunogen  
Keywords  

Notes

Showing 2 of 2 notes.

References

Showing 4 of 4 references.

Ovod1992 V. Ovod, A. Lagerstedt, A. Ranki, F. O. Gombert, R. Spohn, M. Tahtinen, G. Jung, and K. J. Krohn. Immunological Variation and Immunohistochemical Localization of HIV-1 Nef Demonstrated with Monoclonal Antibodies. AIDS, 6:25-34, 1992. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 1371924. Show all entries for this paper.

Ranki1994 A. Ranki, A. Lagerstedt, V. Ovod, E. Aavik, and K. Krohn. Expression Kinetics and Subcellular Localization of HIV-1 Regulatory Proteins Nef and Tat in Established Lymphoid Cell Lines. Arch. Virol., 139:365-378, 1994. PubMed ID: 7832642. Show all entries for this paper.

Ranki1995 A. Ranki, M. Nyberg, V. Ovod, M. Haltia, I. Elovaara, R. Raininko, H. Haapasalo, and K. Krohn. Abundant Expression of HIV Nef and Rev Proteins in Brain Astrocytes In Vivo Is Associated with Dementia. AIDS, 9:1001-1008, 1995. HIV Nef protein was found in the brain cells of infected individuals with clinical neurological disease. PubMed ID: 8527071. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 244

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MAb ID 3H6
HXB2 Location Rev(38-43)
DNA(8414..8431)
Rev Epitope Map
Author Location Rev(38-44)
Epitope RRNRRR Epitope Alignment
RRNRRR epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody generation

Vaccine Details

Vaccine type protein
Vaccine component Rev

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 references.

Isolation Paper
Orsini1995 M. J. Orsini, A. N. Thakur, W. W. Andrews, M.-L. Hammarskjold, and D. Rekosh. Expression and Purification of the HIV Type 1 Rev Protein Produced in Escherichia coli and Its Use in the Generation of Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 11:945-953, 1995. PubMed ID: 7492441. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 247

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MAb ID 8E7
HXB2 Location Rev(70-84)
DNA(8510..8554)
Rev Epitope Map
Author Location Rev(70-84)
Epitope PVPLQLPPLERLTLD Epitope Alignment
PVPLQLPPLERLTLD epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG2aκ)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Rev

Notes

Showing 4 of 4 notes.

References

Showing 6 of 6 references.

Kalland1994 K. H. Kalland, A. M Szilvay, K. A. Brokstad, W. Saetrevik, and G. Haukenes. The Human Immunodeficiency Virus Type 1 Rev Protein Shuttles between the Cytoplasm and Nuclear Compartments. Mol. Cell Biol., 14:7436-7444, 1994. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 7935458. Show all entries for this paper.

Kalland1994a K. H. Kalland, A. M Szilvay, E. Langhoff, and G. Haukenes. Subcellular Distribution of Human Immunodeficiency Virus Type 1 Rev and Colocalization of Rev with RNA Splicing Factors in a Speckled Pattern in the Nucleoplasm. J. Virol., 68:1475-1485, 1994. PubMed ID: 8107211. Show all entries for this paper.

Szilvay1995 A. M. Szilvay, K. A. Brokstad, R. Kopperud, G. Haukenes, and K. H. Kalland. Nuclear Export of the Human Immunodeficiency Virus Type 1 Nucleocytoplasmic Shuttle Protein Rev Is Mediated by Its Activation Domain and Is Blocked by Transdominant Negative Mutants. J. Virol., 69:3315-3323, 1995. PubMed ID: 7745679. Show all entries for this paper.

Jensen1997 T. H. Jensen, A. Jensen, A. M. Szilvay, and J. Kjems. Probing the Structure of HIV-1 Rev by Protein Footprinting of Multiple Monoclonal Antibody-Binding Sites. FEBS Lett., 414:50-54, 1997. Rev was mapped using MAb protein footprinting, which gave results that agreed well with peptide mapping, but was useful for identifying a discontinuous interaction between two regions. Footprints supported a previously proposed structure (Auer et al., Biochemistry, 33 (1994) 2988-2996) predicting that a helix-loop-helix motif in Rev brings the termini of the protein into proximity. PubMed ID: 9305730. Show all entries for this paper.

Boe1998 S. O. Boe, B. Bjorndal, B. Rosok, A. M. Szilvay, and K. H. Kalland. Subcellular Localization of Human Immunodeficiency Virus Type 1 RNAs, Rev, and the Splicing Factor SC-35. Virology, 244:473-482, 1998. PubMed ID: 9601515. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 246

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MAb ID 9G2 (9G2G4D6E8)
HXB2 Location Rev(70-84)
DNA(8510..8554)
Rev Epitope Map
Author Location Rev(70-84)
Research Contact Anne Marie Szilvay
Epitope PVPLQLPPLERLTLD Epitope Alignment
PVPLQLPPLERLTLD epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG2aκ)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Rev

Notes

Showing 4 of 4 notes.

References

Showing 3 of 3 references.

Kalland1994 K. H. Kalland, A. M Szilvay, K. A. Brokstad, W. Saetrevik, and G. Haukenes. The Human Immunodeficiency Virus Type 1 Rev Protein Shuttles between the Cytoplasm and Nuclear Compartments. Mol. Cell Biol., 14:7436-7444, 1994. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 7935458. Show all entries for this paper.

Jensen1997 T. H. Jensen, A. Jensen, A. M. Szilvay, and J. Kjems. Probing the Structure of HIV-1 Rev by Protein Footprinting of Multiple Monoclonal Antibody-Binding Sites. FEBS Lett., 414:50-54, 1997. Rev was mapped using MAb protein footprinting, which gave results that agreed well with peptide mapping, but was useful for identifying a discontinuous interaction between two regions. Footprints supported a previously proposed structure (Auer et al., Biochemistry, 33 (1994) 2988-2996) predicting that a helix-loop-helix motif in Rev brings the termini of the protein into proximity. PubMed ID: 9305730. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 248

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MAb ID Ab4
HXB2 Location Rev(72-91)
DNA(8516..8575)
Rev Epitope Map
Author Location Rev(72-91 BRU)
Research Contact Tony Lowe and Jonathan Karn, MRC Center, Cambridge
Epitope PLQLPPLERLTLDCNEDCGT Epitope Alignment
PLQLPPLERLTLDCNEDCGT epitope logo
Ab Type  
Neutralizing  
Species (Isotype) (IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Rev

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Henderson1997 B. R. Henderson and P. Percipalle. Interactions between HIV Rev and Nuclear Import and Export Factors: The Rev Nuclear Localisation Signal Mediates Specific Binding to Human Importin-beta. J. Mol. Biol., 274:693-707, 1997. PubMed ID: 9405152. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 256

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MAb ID 7E2/4
HXB2 Location gp160(31-50)
DNA(6315..6374)
gp160 Epitope Map
Author Location gp120(31-50 LAI)
Research Contact S. Ranjbar, NIBSC, UK
Epitope TEKLWVTVYYGVPVWKEATT Epitope Alignment
TEKLWVTVYYGVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 258

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MAb ID 4D4#85
HXB2 Location gp160(41-50)
DNA(6345..6374)
gp160 Epitope Map
Author Location gp120( LAI)
Research Contact S. Nigida and L. Arthur, NCI, Frederick, MD USA
Epitope GVPVWKEATT Epitope Alignment
GVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody polyreactivity, immunotherapy

Vaccine Details

Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 6 of 6 notes.

References

Showing 7 of 7 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Moore1996 J. P. Moore and J. Sodroski. Antibody cross-competition analysis of the human immunodeficiency virus type 1 gp120 exterior envelope glycoprotein. J. Virol., 70:1863-1872, 1996. 46 anti-gp120 monomer MAbs were used to create a competition matrix, and MAb competition groups were defined. The data suggests that there are two faces of the gp120 glycoprotein: a face occupied by the CD4BS, which is presumably also exposed on the oligomeric envelope glycoprotein complex, and a second face which is presumably inaccessible on the oligomer and interacts with a number of nonneutralizing antibodies. PubMed ID: 8627711. Show all entries for this paper.

Wyatt1997 R. Wyatt, E. Desjardin, U. Olshevsky, C. Nixon, J. Binley, V. Olshevsky, and J. Sodroski. Analysis of the Interaction of the Human Immunodeficiency Virus Type 1 gp120 Envelope Glycoprotein with the gp41 Transmembrane Glycoprotein. J. Virol., 71:9722-9731, 1997. This study characterized the binding of gp120 and gp41 by comparing Ab reactivity to soluble gp120 and to a soluble complex of gp120 and gp41 called sgp140. The occlusion of gp120 epitopes in the sgp140 complex provides a guide to the gp120 domains that interact with gp41, localizing them in C1 and C5 of gp120. Mutations that disrupt the binding of the occluded antibodies do not influence NAb binding or CD4 binding, thus if the gp41 binding domain is deleted, the immunologically desirable features of gp120 for vaccine design are still intact. PubMed ID: 9371638. Show all entries for this paper.

Binley1998 J. M. Binley, R. Wyatt, E. Desjardins, P. D. Kwong, W. Hendrickson, J. P. Moore, and J. Sodroski. Analysis of the Interaction of Antibodies with a Conserved Enzymatically Deglycosylated Core of the HIV Type 1 Envelope Glycoprotein 120. AIDS Res. Hum. Retroviruses, 14:191-198, 1998. This paper helped showed the biological relevance of a deglycosylated variable loop deleted form of the core gp120. PubMed ID: 9491908. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.


Displaying record number 257

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MAb ID M92
HXB2 Location gp160(41-50)
DNA(6345..6374)
gp160 Epitope Map
Author Location gp120(31-50 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope GVPVWKEATT Epitope Alignment
GVPVWKEATT epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) rat(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 260

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MAb ID M86
HXB2 Location gp160(42-61)
DNA(6348..6407)
gp160 Epitope Map
Author Location gp120(42-61 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope VPVWKEATTTLFCASDAKAY Epitope Alignment
VPVWKEATTTLFCASDAKAY epitope logo
Subtype B
Ab Type gp120 C1
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 325

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MAb ID 697-D (697D, 697-30D)
HXB2 Location gp160(161-180)
DNA(6705..6764)
gp160 Epitope Map
Author Location gp120(161-180 IIIB)
Research Contact Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center) or Cellular Products Inc, Buffalo NY
Epitope ISTSIRGKVQKEYAFFYKLD Epitope Alignment
ISTSIRGKVQKEYAFFYKLD epitope logo
Ab Type gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing P (weak)  View neutralization details
Contacts and Features View contacts and features
Species (Isotype) human(IgG1λ)
Patient  
Immunogen HIV-1 infection
Keywords ADCC, antibody binding site, antibody generation, binding affinity, co-receptor, dendritic cells, enhancing activity, glycosylation, neutralization, review, structure, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity

Notes

Showing 29 of 29 notes.

References

Showing 30 of 30 references.

Isolation Paper
Gorny1994 M. K. Gorny, J. P. Moore, A. J. Conley, S. Karwowska, J. Sodroski, C. Williams, S. Burda, L. J. Boots, and S. Zolla-Pazner. Human Anti-V2 Monoclonal Antibody That Neutralizes Primary but Not Laboratory Isolates of Human Immunodeficiency Virus Type 1. J. Virol., 68:8312-8320, 1994. Detailed characterization of the MAb 697-D. PubMed ID: 7525987. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Bradley2016a Todd Bradley, Ashley Trama, Nancy Tumba, Elin Gray, Xiaozhi Lu, Navid Madani, Fatemeh Jahanbakhsh, Amanda Eaton, Shi-Mao Xia, Robert Parks, Krissey E. Lloyd, Laura L. Sutherland, Richard M. Scearce, Cindy M. Bowman, Susan Barnett, Salim S. Abdool-Karim, Scott D. Boyd, Bruno Melillo, Amos B. Smith, 3rd., Joseph Sodroski, Thomas B. Kepler, S. Munir Alam, Feng Gao, Mattia Bonsignori, Hua-Xin Liao, M Anthony Moody, David Montefiori, Sampa Santra, Lynn Morris, and Barton F. Haynes. Amino Acid Changes in the HIV-1 gp41 Membrane Proximal Region Control Virus Neutralization Sensitivity. EBioMedicine, 12:196-207, Oct 2016. PubMed ID: 27612593. Show all entries for this paper.

EdwardsBH2002 Bradley H. Edwards, Anju Bansal, Steffanie Sabbaj, Janna Bakari, Mark J. Mulligan, and Paul A. Goepfert. Magnitude of Functional CD8+ T-Cell Responses to the Gag Protein of Human Immunodeficiency Virus Type 1 Correlates Inversely with Viral Load in Plasma. J. Virol., 76(5):2298-2305, Mar 2002. PubMed ID: 11836408. Show all entries for this paper.

Forthal1995 D. N. Forthal, G. Landucci, M. K. Gorny, S. Zolla-Pazner, and W. E. Robinson, Jr. Functional Activities of 20 Human Immunodeficiency Virus Type 1 (HIV-1)-Specific Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 11:1095-1099, 1995. A series of tests were performed on 20 human monoclonal antibodies to assess their potential therapeutic utility. Antibodies were tested for potentially harmful complement-mediated antibody enhancing activity (C-ADE), and for potentially beneficial neutralizing activity and antibody dependent cellular cytotoxicity ADCC. PubMed ID: 8554906. Show all entries for this paper.

Fouts1997 T. R. Fouts, J. M. Binley, A. Trkola, J. E. Robinson, and J. P. Moore. Neutralization of the Human Immunodeficiency Virus Type 1 Primary Isolate JR-FL by Human Monoclonal Antibodies Correlates with Antibody Binding to the Oligomeric Form of the Envelope Glycoprotein Complex. J. Virol., 71:2779-2785, 1997. To test whether antibody neutralization of HIV-1 primary isolates is correlated with the affinities for the oligomeric envelope glycoproteins, JRFL was used as a model primary virus and a panel of 13 human MAbs were evaluated for: half-maximal binding to rec monomeric JRFL gp120; half-maximal binding to oligomeric - JRFL Env expressed on the surface of transfected 293 cells; and neutralization of JRFL in a PBMC-based neutralization assay. Antibody affinity for oligomeric JRFL Env but not monomeric JRFL gp120 correlated with JRFL neutralization. PubMed ID: 9060632. Show all entries for this paper.

Gorny2000b M. K. Gorny, T. C. VanCott, C. Williams, K. Revesz, and S. Zolla-Pazner. Effects of oligomerization on the epitopes of the human immunodeficiency virus type 1 envelope glycoproteins. Virology, 267:220-8, 2000. PubMed ID: 10662617. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Gorny2012 Miroslaw K. Gorny, Ruimin Pan, Constance Williams, Xiao-Hong Wang, Barbara Volsky, Timothy O'Neal, Brett Spurrier, Jared M. Sampson, Liuzhe Li, Michael S. Seaman, Xiang-Peng Kong, and Susan Zolla-Pazner. Functional and Immunochemical Cross-Reactivity of V2-Specific Monoclonal Antibodies from HIV-1-Infected Individuals. Virology, 427(2):198-207, 5 Jun 2012. PubMed ID: 22402248. Show all entries for this paper.

Granados-Gonzalez2008 Viviana Granados-Gonzalez, Julien Claret, Willy Berlier, Nadine Vincent, Silvio Urcuqui-Inchima, Frederic Lucht, Christiane Defontaine, Abraham Pinter, Christian Genin, and Serge Riffard. Opposite Immune Reactivity of Serum IgG and Secretory IgA to Conformational Recombinant Proteins Mimicking V1/V2 Domains of Three Different HIV Type 1 Subtypes Depending on Glycosylation. AIDS Res. Hum. Retroviruses, 24(2):289-299, Feb 2008. PubMed ID: 18260782. Show all entries for this paper.

Haldar2011 Bijayesh Haldar, Sherri Burda, Constance Williams, Leo Heyndrickx, Guido Vanham, Miroslaw K. Gorny, and Phillipe Nyambi. Longitudinal Study of Primary HIV-1 Isolates in Drug-Naïve Individuals Reveals the Emergence of Variants Sensitive to Anti-HIV-1 Monoclonal Antibodies. PLoS One, 6(2):e17253, 2011. PubMed ID: 21383841. Show all entries for this paper.

He2002 Yuxian He, William J. Honnen, Chavdar P. Krachmarov, Michael Burkhart, Samuel C. Kayman, Jose Corvalan, and Abraham Pinter. Efficient Isolation of Novel Human Monoclonal Antibodies with Neutralizing Activity Against HIV-1 from Transgenic Mice Expressing Human Ig Loci. J. Immunol., 169(1):595-605, 1 Jul 2002. PubMed ID: 12077293. Show all entries for this paper.

Hioe2000 C. E. Hioe, G. J. Jones, A. D. Rees, S. Ratto-Kim, D. Birx, C. Munz, M. K. Gorny, M. Tuen, and S. Zolla-Pazner. Anti-CD4-Binding Domain Antibodies Complexed with HIV Type 1 Glycoprotein 120 Inhibit CD4+ T Cell-Proliferative Responses to Glycoprotein 120. AIDS Res. Hum. Retroviruses, 16:893-905, 2000. PubMed ID: 10875615. Show all entries for this paper.

Hioe2009 Catarina E. Hioe, Maria Luisa Visciano, Rajnish Kumar, Jianping Liu, Ethan A. Mack, Rachel E. Simon, David N. Levy, and Michael Tuen. The Use of Immune Complex Vaccines to Enhance Antibody Responses against Neutralizing Epitopes on HIV-1 Envelope gp120. Vaccine, 28(2):352-360, 11 Dec 2009. PubMed ID: 19879224. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Kalia2005 Vandana Kalia, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41. J. Virol., 79(4):2097-2107, Feb 2005. PubMed ID: 15681412. Show all entries for this paper.

Kramer2007 Victor G. Kramer, Nagadenahalli B. Siddappa, and Ruth M. Ruprecht. Passive Immunization as Tool to Identify Protective HIV-1 Env Epitopes. Curr. HIV Res., 5(6):642-55, Nov 2007. PubMed ID: 18045119. Show all entries for this paper.

Liao2013b Hua-Xin Liao, Mattia Bonsignori, S. Munir Alam, Jason S. McLellan, Georgia D. Tomaras, M. Anthony Moody, Daniel M. Kozink, Kwan-Ki Hwang, Xi Chen, Chun-Yen Tsao, Pinghuang Liu, Xiaozhi Lu, Robert J. Parks, David C. Montefiori, Guido Ferrari, Justin Pollara, Mangala Rao, Kristina K. Peachman, Sampa Santra, Norman L. Letvin, Nicos Karasavvas, Zhi-Yong Yang, Kaifan Dai, Marie Pancera, Jason Gorman, Kevin Wiehe, Nathan I. Nicely, Supachai Rerks-Ngarm, Sorachai Nitayaphan, Jaranit Kaewkungwal, Punnee Pitisuttithum, James Tartaglia, Faruk Sinangil, Jerome H. Kim, Nelson L. Michael, Thomas B. Kepler, Peter D. Kwong, John R. Mascola, Gary J. Nabel, Abraham Pinter, Susan Zolla-Pazner, and Barton F. Haynes. Vaccine Induction of Antibodies Against a Structurally Heterogeneous Site of Immune Pressure within HIV-1 Envelope Protein Variable Regions 1 and 2. Immunity, 38(1):176-186, 24 Jan 2013. PubMed ID: 23313589. Show all entries for this paper.

Liu2014 Pinghuang Liu, Latonya D. Williams, Xiaoying Shen, Mattia Bonsignori, Nathan A. Vandergrift, R. Glenn Overman, M. Anthony Moody, Hua-Xin Liao, Daniel J. Stieh, Kerrie L. McCotter, Audrey L. French, Thomas J. Hope, Robin Shattock, Barton F. Haynes, and Georgia D. Tomaras. Capacity for Infectious HIV-1 Virion Capture Differs by Envelope Antibody Specificity. J. Virol., 88(9):5165-5170, May 2014. PubMed ID: 24554654. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

McCann2005 C. M. Mc Cann, R. J. Song, and R. M. Ruprecht. Antibodies: Can They Protect Against HIV Infection? Curr. Drug Targets Infect. Disord., 5(2):95-111, Jun 2005. PubMed ID: 15975016. Show all entries for this paper.

Moore1995c J. P. Moore and D. D. Ho. HIV-1 Neutralization: The Consequences of Adaptation to Growth on Transformed T-Cells. AIDS, 9(suppl A):S117-S136, 1995. This review considers the relative importance of a neutralizing antibody response for the development of a vaccine, and for disease progression during the chronic phase of HIV-1 infection. It suggests that T-cell immunity may be more important. The distinction between MAbs that can neutralize primary isolates, and those that are effective at neutralizing only laboratory adapted strains is discussed in detail. Alternative conformations of envelope and non-contiguous interacting domains in gp120 are discussed. The suggestion that soluble monomeric gp120 may serve as a viral decoy that diverts the humoral immune response it in vivo is put forth. PubMed ID: 8819579. Show all entries for this paper.

Nyambi1998 P. N. Nyambi, M. K. Gorny, L. Bastiani, G. van der Groen, C. Williams, and S. Zolla-Pazner. Mapping of Epitopes Exposed on Intact Human Immunodeficiency Virus Type 1 (HIV-1) Virions: A New Strategy for Studying the Immunologic Relatedness of HIV-1. J. Virol., 72:9384-9391, 1998. 18 human MAbs binding to gp120 and gp41 were tested using a novel assay to test binding to intact HIV-1 virions. The new method involves using MAbs to the host proteins incorporated into virions to bind them to ELIZA plates. Antigenic conservation in epitopes of HIV-1 in clades A, B, D, F, G, and H was studied. MAbs were selected that were directed against V2, V3, CD4bd, C5 or gp41 regions. Antibodies against V2, the CD4BS, and sp41 showed weak and sporadic reactivities, while binding strongly to gp120, suggesting these epitopes are hidden when gp120 is in its native, quaternary structure. PubMed ID: 9765494. Show all entries for this paper.

Nyambi2000 P. N. Nyambi, H. A. Mbah, S. Burda, C. Williams, M. K. Gorny, A. Nadas, and S. Zolla-Pazner. Conserved and Exposed Epitopes on Intact, Native, Primary Human Immunodeficiency Virus Type 1 Virions of Group M. J. Virol., 74:7096-7107, 2000. PubMed ID: 10888650. Show all entries for this paper.

Parren1997 P. W. Parren, M. C. Gauduin, R. A. Koup, P. Poignard, Q. J. Sattentau, P. Fisicaro, and D. R. Burton. Erratum to Relevance of the Antibody Response against Human Immunodeficiency Virus Type 1 Envelope to Vaccine Design. Immunol. Lett., 58:125-132, 1997. corrected and republished article originally printed in Immunol. Lett. 1997 Jun;57(1-3):105-112. PubMed ID: 9271324. Show all entries for this paper.

Selvarajah2005 Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142. Show all entries for this paper.

Stamatatos1998 L. Stamatatos and C. Cheng-Mayer. An Envelope Modification That Renders a Primary, Neutralization-Resistant Clade B Human Immunodeficiency Virus Type 1 Isolate Highly Susceptible to Neutralization by Sera from Other Clades. J. Virol., 72:7840-7845, 1998. PubMed ID: 9733820. Show all entries for this paper.

Trkola1996b A. Trkola, T. Dragic, J. Arthos, J. M. Binley, W. C. Olson, G. P. Allaway, C. Cheng-Mayer, J. Robinson, P. J. Maddon, and J. P. Moore. CD4-Dependent, Antibody-Sensitive Interactions between HIV-1 and Its Co-Receptor CCR-5. Nature, 384:184-187, 1996. CCR-5 is a co-factor for fusion of HIV-1 strains of the non-syncytium-inducing (NSI) phenotype with CD4+ T-cells. CD4 binding greatly increases the efficiency of gp120-CCR-5 interaction. Neutralizing MAbs against the V3 loop and CD4-induced epitopes on gp120 inhibited the interaction of gp120 with CCR-5, without affecting gp120-CD4 binding. PubMed ID: 8906796. Show all entries for this paper.

Upadhyay2014 Chitra Upadhyay, Luzia M. Mayr, Jing Zhang, Rajnish Kumar, Miroslaw K. Gorny, Arthur Nádas, Susan Zolla-Pazner, and Catarina E. Hioe. Distinct Mechanisms Regulate Exposure of Neutralizing Epitopes in the V2 and V3 Loops of HIV-1 Envelope. J. Virol., 88(21):12853-12865, Nov 2014. PubMed ID: 25165106. Show all entries for this paper.

Yates2018 Nicole L. Yates, Allan C. deCamp, Bette T. Korber, Hua-Xin Liao, Carmela Irene, Abraham Pinter, James Peacock, Linda J. Harris, Sheetal Sawant, Peter Hraber, Xiaoying Shen, Supachai Rerks-Ngarm, Punnee Pitisuttithum, Sorachai Nitayapan, Phillip W. Berman, Merlin L. Robb, Giuseppe Pantaleo, Susan Zolla-Pazner, Barton F. Haynes, S. Munir Alam, David C. Montefiori, and Georgia D. Tomaras. HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees. J. Virol., 92(8), 15 Apr 2018. PubMed ID: 29386288. Show all entries for this paper.


Displaying record number 1067

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MAb ID 8.22.2 (Xeno-mAb 8.22.2)
HXB2 Location gp160(162-178)
DNA(6708..6758)
gp160 Epitope Map
Author Location gp120(gp120 )
Research Contact Dr. Abraham Pinter, Public Health Research Institute, Newark, NJ, pinter@phri.org
Epitope TTSIRDKVQKEYALFYK Epitope Alignment
TTSIRDKVQKEYALFYK epitope logo
Ab Type gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing  
Species (Isotype) transgenic mouse(IgG2κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, neutralization, review, subtype comparisons, vaccine antigen design, vaccine-induced immune responses, variant cross-reactivity

Vaccine Details

Vaccine type protein
Vaccine strain B clade SF162
Vaccine component gp120
Adjuvant Ribi adjuvant (MPL+TDM) (RIBI)

Notes

Showing 8 of 8 notes.

References

Showing 8 of 8 references.

Isolation Paper
He2002 Yuxian He, William J. Honnen, Chavdar P. Krachmarov, Michael Burkhart, Samuel C. Kayman, Jose Corvalan, and Abraham Pinter. Efficient Isolation of Novel Human Monoclonal Antibodies with Neutralizing Activity Against HIV-1 from Transgenic Mice Expressing Human Ig Loci. J. Immunol., 169(1):595-605, 1 Jul 2002. PubMed ID: 12077293. Show all entries for this paper.

Dhillon2007 Amandeep K. Dhillon, Helen Donners, Ralph Pantophlet, Welkin E. Johnson, Julie M. Decker, George M. Shaw, Fang-Hua Lee, Douglas D. Richman, Robert W. Doms, Guido Vanham, and Dennis R. Burton. Dissecting the Neutralizing Antibody Specificities of Broadly Neutralizing Sera from Human Immunodeficiency Virus Type 1-Infected Donors. J. Virol., 81(12):6548-6562, Jun 2007. PubMed ID: 17409160. Show all entries for this paper.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this paper.

Granados-Gonzalez2008 Viviana Granados-Gonzalez, Julien Claret, Willy Berlier, Nadine Vincent, Silvio Urcuqui-Inchima, Frederic Lucht, Christiane Defontaine, Abraham Pinter, Christian Genin, and Serge Riffard. Opposite Immune Reactivity of Serum IgG and Secretory IgA to Conformational Recombinant Proteins Mimicking V1/V2 Domains of Three Different HIV Type 1 Subtypes Depending on Glycosylation. AIDS Res. Hum. Retroviruses, 24(2):289-299, Feb 2008. PubMed ID: 18260782. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Pantophlet2004 R. Pantophlet, I. A. Wilson, and D. R. Burton. Improved Design of an Antigen with Enhanced Specificity for the Broadly HIV-Neutralizing Antibody b12. Protein Eng. Des. Sel., 17(10):749-758, Oct 2004. PubMed ID: 15542540. Show all entries for this paper.

Pinter2004 Abraham Pinter, William J. Honnen, Yuxian He, Miroslaw K. Gorny, Susan Zolla-Pazner, and Samuel C. Kayman. The V1/V2 Domain of gp120 Is a Global Regulator of the Sensitivity of Primary Human Immunodeficiency Virus Type 1 Isolates to Neutralization by Antibodies Commonly Induced upon Infection. J. Virol., 78(10):5205-5215, May 2004. PubMed ID: 15113902. Show all entries for this paper.

Selvarajah2005 Suganya Selvarajah, Bridget Puffer, Ralph Pantophlet, Mansun Law, Robert W. Doms, and Dennis R. Burton. Comparing Antigenicity and Immunogenicity of Engineered gp120. J. Virol., 79(19):12148-12163, Oct 2005. PubMed ID: 16160142. Show all entries for this paper.


Displaying record number 326

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MAb ID 12b
HXB2 Location gp160(162-181)
DNA(6708..6767)
gp160 Epitope Map
Author Location gp120(162-181)
Epitope STSIRGKVQKEYAFFYKLDI Epitope Alignment
STSIRGKVQKEYAFFYKLDI epitope logo
Ab Type gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing L (HXB10)
Species (Isotype) rat(IgG2a)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BH10
Vaccine component gp120

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Shotton1995 C. Shotton, C. Arnold, Q. Sattentau, J. Sodroski, and J. A. McKeating. Identification and characterization of monoclonal antibodies specific for polymorphic antigenic determinants within the V2 region of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol., 69:222-230, 1995. Anti-V2 linear and conformation dependent MAbs were studied. All V2 Abs studied could bind IIIB, but failed to neutralize non-clonal stocks. Epitope exposure is different in rgp120 compared to native gp120. HXB2 V2-MAb neutralization escape mutants were sequenced. PubMed ID: 7527084. Show all entries for this paper.

McKeating1996b J. A. McKeating, Y. J. Zhang, C. Arnold, R. Frederiksson, E. M. Fenyo, and P. Balfe. Chimeric viruses expressing primary envelope glycoproteins of human immunodeficiency virus type I show increased sensitivity to neutralization by human sera. Virology, 220:450-460, 1996. Chimeric viruses for HXB2 with primary isolate gp120 gave patterns of cell tropism and cytopathicity identical to the original primary viruses. Sera that were unable to neutralize the primary isolates were in some cases able to neutralize chimeric viruses, indicating that some of the neutralizing epitopes were in gp41. PubMed ID: 8661395. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 365

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MAb ID B12
HXB2 Location gp160(252-271)
DNA(6978..7037)
gp160 Epitope Map
Author Location gp120(252-271 LAI)
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords antibody generation

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 4 of 4 notes.

References

Showing 3 of 3 references.

Isolation Paper
Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.


Displaying record number 364

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MAb ID M89
HXB2 Location gp160(252-271)
DNA(6978..7037)
gp160 Epitope Map
Author Location gp120(252-271 LAI)
Research Contact Fulvia di Marzo Veronese
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Env

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Veronese1992 F. di Marzo Veronese, R. Rahman, R. Pal, C. Boyer, J. Romano, V. S. Kalyanaraman, B. C. Nair, R. C. Gallo, and M. G. Sarngadharan. Delineation of immunoreactive, conserved regions in the external envelope glycoprotein of the human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 8:1125-1132, 1992. PubMed ID: 1380259. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 375

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MAb ID C13
HXB2 Location gp160(252-271)
DNA(6978..7037)
gp160 Epitope Map
Author Location gp120(252-271 LAI)
Research Contact George Lewis
Epitope RPVVSTQLLLNGSLAEEEVV Epitope Alignment
RPVVSTQLLLNGSLAEEEVV epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component gp160

Notes

Showing 5 of 5 notes.

References

Showing 4 of 4 references.

Moore1993a J. P. Moore and D. D. Ho. Antibodies to discontinuous or conformationally sensitive epitopes on the gp120 glycoprotein of human immunodeficiency virus type 1 are highly prevalent in sera of infected humans. J. Virol., 67:863-875, 1993. CD4BS antibodies are prevalent in HIV-1-positive sera, while neutralizing MAbs to C4, V2, and V3 and MAbs to linear epitopes are less common. Most linear epitope MAbs in human sera are directed against the V3 region, and cross-reactive MAbs tend to be directed against discontinuous epitopes. PubMed ID: 7678308. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Abacioglu1994 Y. H. Abacioglu, T. R. Fouts, J. D. Laman, E. Claassen, S. H. Pincus, J. P. Moore, C. A. Roby, R. Kamin-Lewis, and G. K. Lewis. Epitope Mapping and Topology of Baculovirus-Expressed HIV-1 gp160 Determined with a Panel of Murine Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 10:371-381, 1994. Thirty MAbs were obtained from BALB/c mice immunized with rgp160 LAI expressed in baculovirus. These antibodies map to 4 domains: gp120 C1, C2, C3/V4, and the cytoplasmic tail of gp41. All epitopes were exposed on rgp160 without denaturing the protein, but 6/8 epitopes mapped in gp120 are not exposed unless the protein is denatured, showing rgp160 and rgp120 fold differently. PubMed ID: 8068416. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 376

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MAb ID 110.E
HXB2 Location gp160(262-281)
DNA(7008..7067)
gp160 Epitope Map
Author Location gp120(262-281 LAI)
Research Contact F. Traincard
Epitope NGSLAEEEVVIRSVNFTDNA Epitope Alignment
NGSLAEEEVVIRSVNFTDNA epitope logo
Subtype B
Ab Type gp120 C2
Neutralizing  
Species (Isotype) mouse(IgG)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade LAI
Vaccine component Env

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 379

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MAb ID IIIB-V3-26
HXB2 Location gp160(291-307)
DNA(7095..7145)
gp160 Epitope Map
Author Location gp120(299-304 IIIB)
Epitope SVEINCTRPNNNTRKSI Epitope Alignment
SVEINCTRPNNNTRKSI epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain B clade IIIB

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Laman1992 J. D. Laman, M. M. Schellekens, Y. H. Abacioglu, G. K. Lewis, M. Tersmette, R. A. M. Fouchier, J. P. M. Langeduk, E. Claassen, and W. J. A. Boersma. Variant-specific monoclonal and group-specific polyclonal human immunodeficiency virus type 1 neutralizing antibodies raised with synthetic peptides from the gp120 third variable domain. J. Virol., 66:1823-1831, 1992. PubMed ID: 1629971. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 378

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MAb ID IIIB-V3-21 (V3-21, EVA3048)
HXB2 Location gp160(294-299)
DNA(7104..7121)
gp160 Epitope Map
Author Location gp120(299-304 IIIB)
Research Contact J. Laman
Epitope INCTRP Epitope Alignment
INCTRP epitope logo
Ab Type gp120 V3 // V3 glycan (V3g)
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords antibody binding site, co-receptor, dendritic cells, enhancing activity, mimics, neutralization

Vaccine Details

Vaccine type peptide
Vaccine strain B clade IIIB

Notes

Showing 12 of 12 notes.

References

Showing 10 of 10 references.

Laman1992 J. D. Laman, M. M. Schellekens, Y. H. Abacioglu, G. K. Lewis, M. Tersmette, R. A. M. Fouchier, J. P. M. Langeduk, E. Claassen, and W. J. A. Boersma. Variant-specific monoclonal and group-specific polyclonal human immunodeficiency virus type 1 neutralizing antibodies raised with synthetic peptides from the gp120 third variable domain. J. Virol., 66:1823-1831, 1992. PubMed ID: 1629971. Show all entries for this paper.

Laman1993 J. D. Laman, M. M. Schellekens, G. K. Lewis, J. P. Moore, T. J. Matthews, J. P. M. Langedijk, R. H. Meloen, W. J. A. Boersma, and E. Claassen. A Hidden Region in the Third Variable Domain of HIV-1 IIIB gp120 Identified by a Monoclonal Antibody. AIDS Res. Hum. Retroviruses, 9:605-612, 1993. A peptide (FVTIGKIGNMRQAHC) induced MAb binds to the carboxy-terminal flank of the V3-loop, but the epitope is only exposed on gp120 when it is treated with SDS-DTT. PubMed ID: 8369165. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.

Zhang2002 Peng Fei Zhang, Peter Bouma, Eun Ju Park, Joseph B. Margolick, James E. Robinson, Susan Zolla-Pazner, Michael N. Flora, and Gerald V. Quinnan, Jr. A Variable Region 3 (V3) Mutation Determines a Global Neutralization Phenotype and CD4-Independent Infectivity of a Human Immunodeficiency Virus Type 1 Envelope Associated with a Broadly Cross-Reactive, Primary Virus-Neutralizing Antibody Response. J. Virol., 76(2):644-655, Jan 2002. PubMed ID: 11752155. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Ling2004 Hong Ling, Peng Xiao, Osamu Usami, and Toshio Hattori. Thrombin Activates Envelope Glycoproteins of HIV Type 1 and Enhances Fusion. Microbes Infect., 6(5):414-420, Apr 2004. PubMed ID: 15109955. Show all entries for this paper.

vanMontfort2007 Thijs van Montfort, Alexey A. Nabatov, Teunis B. H. Geijtenbeek, Georgios Pollakis, and William A. Paxton. Efficient Capture of Antibody Neutralized HIV-1 by Cells Expressing DC-SIGN and Transfer to CD4+ T Lymphocytes. J. Immunol., 178(5):3177-85, 1 Mar 2007. PubMed ID: 17312166. Show all entries for this paper.

Cadogan2008 Martin Cadogan, Brian Austen, Jonathan L. Heeney, and Angus G. Dalgleish. HLA Homology within the C5 Domain Promotes Peptide Binding by HIV Type 1 gp120. AIDS Res. Hum. Retroviruses, 24(6):845-855, Jun 2008. PubMed ID: 18544021. Show all entries for this paper.

Chomont2008 Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650. Show all entries for this paper.

vanMontfort2008 Thijs van Montfort, Adri A. M. Thomas, Georgios Pollakis, and William A. Paxton. Dendritic Cells Preferentially Transfer CXCR4-Using Human Immunodeficiency Virus Type 1 Variants to CD4+ T Lymphocytes in trans. J. Viro.l, 82(16):7886-7896, Aug 2008. PubMed ID: 18524826. Show all entries for this paper.


Displaying record number 578

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MAb ID M38
HXB2 Location gp160(485-504)
DNA(7677..7736)
gp160 Epitope Map
Author Location gp120(490-508)
Epitope KYKVVKEIPLGVAPTKAKRR Epitope Alignment
KYKVVKEIPLGVAPTKAKRR epitope logo
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type virus
Vaccine strain B clade IIIB
Vaccine component HIV-1

Notes

Showing 4 of 4 notes.

References

Showing 6 of 6 references.

Beretta1987 A. Beretta, F. Grassi, M. Pelagi, A. Clivio, C. Parravicini, G. Giovinazzo, F. Andronico, L. Lopalco, P. Verani, S. Butto, F. Titti, G. B. Rossi, G. Viale, E. Ginelli, and A. G. Siccardi. HIV Env Glycoprotein Shares a Cross-Reacting Epitope with a Surface Protein Present on Activated Human Monocytes and Involved in Antigen Presentation. Eur. J. Immunol., 17:1793-1798, 1987. The MAb M38 binds to gp120 and also to a human protein of 80 kd that is expressed on a small fraction of mononuclear cells in the lymph nodes. M38 inhibits proliferation in autologous tetanus toxoid presentation, so is involved in antigen presentation. Suggested molecular mimicry. PubMed ID: 2446880. Show all entries for this paper.

Grassi1991 F. Grassi, R. Meneveri, M. Gullberg, L. Lopalco, G. B. Rossi, P. Lanza, C. DeSantis, G. Brattsand, S. Butto, E. Ginelli, A. Berretta, and A. G. Siccardi. Human Immunodeficiency Virus Type 1 gp120 Mimics a Hidden Monomorphic Epitope Borne by Class I Major Histocompatibility Complex Heavy Chains. J. Exp. Med., 174:53-62, 1991. PubMed ID: 1711567. Show all entries for this paper.

Lopalco1993 L. Lopalco, R. Longhi, F. Ciccomascolo, A. De Rossi, M. Pelagi, F. Andronico, J. P. Moore, B T. Schulz, A. Beretta, and A. G. Siccardi. Identification of human immunodeficiency virus type 1 glycoprotein gp120/gp41 interacting sites by the idiotypic mimicry of two monoclonal antibodies. AIDS Res. Hum. Retroviruses, 9:33-39, 1993. The MAb M38 binds to the carboxy terminus of gp120, in a gp41 binding region. This MAb was used to create an anti-idiotype MAb, 9G5A, which can bind to gp41 at the base of the cysteine loop. The binding domains of these two monoclonals are consistent with the C5 domain of gp120 being able to bind to the gp41 cysteine loop. The MAb M38 also binds to human HLA molecules, in antigenic homology or possibly molecular mimicry. PubMed ID: 7678970. Show all entries for this paper.

DeSantis1994 C. DeSantis, L. Lopalco, P. Robbioni, R. Longhi, G. Rappocciolo, A. G. Siccardi, and A. Beretta. Human Antibodies to Immunodominant C5 Region of HIV-1 gp120 Cross-React with HLA Class I on Activated Cells. AIDS Res. Hum. Retroviruses, 10:157-162, 1994. PubMed ID: 7515259. Show all entries for this paper.

Beretta1994 A. Beretta and A.G. Dalgleish. B-Cell Epitopes. AIDS, 8(suppl 1):S133-S145, 1994. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 589

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MAb ID polyclonal
HXB2 Location gp160(490-511)
DNA(7692..7757)
gp160 Epitope Map
Author Location gp120(495-516 BRU)
Epitope KIEPLGVAPTKAKRRVVQREKR Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) human
Patient  
Immunogen HIV-1 infection
Keywords  

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Hernandez2000 M. Hernandez, L. Pozo, I. Gomez, and A. Melchor. Chimeric Synthetic Peptide as Antigen for Immunodiagnosis of HIV-1 Infection. Biochem. Biophys. Res. Commun., 272:259-262, 2000. PubMed ID: 10872836. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 581

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MAb ID 110.1 (110-1)
HXB2 Location gp160(491-500)
DNA(7695..7724)
gp160 Epitope Map
Author Location gp120(491-500 LAI)
Research Contact Genetic Systems Corp, Seattle WA, E. Kinney-Thomas
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) mouse(IgG1κ)
Patient  
Immunogen vaccine
Keywords antibody binding site, antibody generation, immunotoxin

Vaccine Details

Vaccine type HIV infected-cell lysate
Vaccine strain B clade BRU
Vaccine component HIV-1

Notes

Showing 11 of 11 notes.

References

Showing 12 of 12 references.

Isolation Paper
Gosting1987 L. H. Gosting, J. McClure, E. S. Dickinson, S. M. Watanabe, K. Shriver, and L. C. Goldstein. Monoclonal antibodies to gp110 and gp41 of human immunodeficiency virus. J. Clin. Microbiol., 25:845-848, 1987. PubMed ID: 2438302. Show all entries for this paper.

Binley1997 J. M. Binley, H. Arshad, T. R. Fouts, and J. P. Moore. An investigation of the high avidity antibody response to gp120 of human immunodeficiency virus type 1. AIDS Res. Hum. Retroviruses, 13:1007-1015, 1997. PubMed ID: 9264287. Show all entries for this paper.

Callahan1991 Lawrence N. Callahan, Michael Phelan, Margherita Mallinson, and Michael A. Norcross. Dextran Sulfate Blocks Antibody Binding to the Principal Neutralizing Domain of Human Immunodeficiency Virus Type 1 without Interfering with gp120-CD4 Interactions. J. Virol., 65(3):1543-1550, Mar 1991. PubMed ID: 1995952. Show all entries for this paper.

Cook1994 D. G. Cook, J. Fantini, S. L. Spitalnik, and F. Gonzalez-Scarano. Binding of Human Immunodeficiency Virus Type 1 HIV-1 gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop. Virol., 201:206-214, 1994. Antibodies against GalCer can block infection of CD4-negative cells from the brain and colon that are susceptible to HIV infection. This paper explores the ability of a panel of MAbs to inhibit binding of gp120 to GalCer, and also of the binding of GalCer to inhibit MAb-gp120 interaction. MAbs to the V3 loop and GalCer showed mutual inhibition of binding to gp120, and anti-CD4 binding site MAbs showed reduced inhibition. N- and C-terminal MAbs didn't influence GalCer binding. PubMed ID: 8184533. Show all entries for this paper.

Kanduc2008 Darja Kanduc, Rosario Serpico, Alberta Lucchese, and Yehuda Shoenfeld. Correlating Low-Similarity Peptide Sequences and HIV B-Cell Epitopes. Autoimmun. Rev., 7(4):291-296, Feb 2008. PubMed ID: 18295732. Show all entries for this paper.

Linsley1988 P. S. Linsley, J. A. Ledbetter, E. Kinney-Thomas, and S.-L. Hu. Effects of Anti-gp120 Monoclonal Antibodies on CD4 Receptor Binding by the env Protein of Human Immunodeficiency Virus Type 1. J. Virol., 62:3695-3702, 1988. PubMed ID: 2458487. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

McDougal1996 J. S. McDougal, M. S. Kennedy, S. L. Orloff, J. K. A. Nicholson, and T. J. Spira. Mechanisms of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralization: Irreversible Inactivation of Infectivity by Anti-HIV-1 Antibody. J. Virol., 70:5236-5245, 1996. Studies of polyclonal sera autologous virus inactivation indicates that in individuals over time, viral populations emerge that are resistant to inactivating effects of earlier sera. PubMed ID: 8764033. Show all entries for this paper.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Pincus1991 S. H. Pincus, R. L. Cole, E. M. Hersh, D. Lake, Y. Masuho, P. J. Durda, and J. McClure. In Vitro Efficacy of Anti-HIV Immunotoxins Targeted by Various Antibodies to the Envelope Protein. J. Immunol., 146:4315-4324, 1991. Six MAbs, (907, 924, 110.1, 41.1, 86 and P5-3) and polyclonal pooled serum antibodies purified on gp160 were coupled to RAC to create immunotoxins. Only 41.1-RAC, an anti-gp41 MAb-immunotoxin and the polyclonal immunotoxin showed direct activity against multiple strains, and activity of an immunotoxin was found not to be directly correlated with cell surface binding. PubMed ID: 1710247. Show all entries for this paper.

Thomas1988 E. Kinney Thomas, J. N. Weber, J. McClure, P. R. Clapham, M. C. Singhal, M. K. Shriver, and R. A. Weiss. Neutralizing Monoclonal Antibodies to the AIDS Virus. AIDS, 2:25-29, 1988. PubMed ID: 2451922. Show all entries for this paper.

Valenzuela1998 A. Valenzuela, J. Blanco, B. Krust, R. Franco, and A. G. Hovanessian. Neutralizing Antibodies against the V3 Loop of Human Immunodeficiency Type 1 gp120 Block the CD4-Dependent and Independent Binding of the Virus to Cells. J. Virol., 71:8289-8298, 1998. PubMed ID: 9343181. Show all entries for this paper.


Displaying record number 580

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MAb ID RV110026
HXB2 Location gp160(491-500)
DNA(7695..7724)
gp160 Epitope Map
Author Location gp120(491-500 LAI)
Research Contact Commercial, Olympus Inc
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) human
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type peptide
Vaccine strain B clade LAI

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Moore1994a J. P. Moore, Q. J. Sattentau, R. Wyatt, and J. Sodroski. Probing the Structure of the Human Immunodeficiency Virus Surface Glycoprotein gp120 with a Panel of Monoclonal Antibodies. J. Virol., 68:469-484, 1994. This study compared a large number of MAbs that bind to linear epitopes of gp120, and compared binding affinities for: i) native and SDS-DDT denatured gp120, (clone BH10 of the LAI isolate expressed in CHO cells); ii) recombinant gp120 lacking the V1, V2, V3 loops; iii) a panel of 20 mer peptides; iv) a panel of gp120 mutants; and v) oligomeric versus monomeric gp120. The binding ratio of native versus denatured monomeric gp120 is included in the table in this database. These numbers should be considered with the following points in mind: a continuous epitope may be partially exposed on the surface; and a preparation of rgp120 is not homogeneous and contains fully folded, partly denatured, and some completely unfolded species, so the conformation of what is considered to be a native protein will not only reflect fully folded gp120. The authors suggest that a fivefold increase in the affinity for a MAb binding to denatured versus native gp120 indicates that the epitope is inaccessible in the native form. We also have included here information extracted from Moore et al's list of the gp120 mutations that reduced the binding of a particular MAb. In mapping of exposed regions of gp120, C2, C3, and C5 domain epitopes were found to bind preferentially to denatured gp120. V1, V2 and V3, part of C4, and the extreme carboxy terminus of C5 were exposed on the native monomer. In the oligomeric form of the molecule, only V2, V3 and part of C4 are well exposed as continuous epitopes. PubMed ID: 7504741. Show all entries for this paper.

Moore1994c J. P. Moore, R. L. Willey, G. K. Lewis, J. Robinson, and J. Sodroski. Immunological evidence for interactions between the first, second and fifth conserved domains of the gp120 surface glycoprotein of human immunodeficiency virus type 1. J. Virol., 68:6836-6847, 1994. Mutation 267N/Q in C2 region results in exposing the carboxy-terminal end gp120. PubMed ID: 7933065. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 577

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MAb ID 43F
HXB2 Location gp160(491-500)
DNA(7695..7724)
gp160 Epitope Map
Author Location gp120(491-500 HXB2)
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) human(IgG1λ)
Patient  
Immunogen HIV-1 infection
Keywords ADCC, review

Notes

Showing 3 of 3 notes.

References

Showing 3 of 3 references.

Alsmadi1997 O. Alsmadi, R. Herz, E. Murphy, A. Pinter, and S. A. Tilley. A novel antibody-dependent cellular cytotoxicity epitope in gp120 is identified by two monoclonal antibodies isolated from a long-term survivor of human immunodeficiency virus type 1 infection. J. Virol., 71:925-33, 1997. PubMed ID: 8995609. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Pollara2013 Justin Pollara, Mattia Bonsignori, M. Anthony Moody, Marzena Pazgier, Barton F. Haynes, and Guido Ferrari. Epitope Specificity of Human Immunodeficiency Virus-1 Antibody Dependent Cellular Cytotoxicity (ADCC) Responses. Curr. HIV Res., 11(5):378-387, Jul 2013. PubMed ID: 24191939. Show all entries for this paper.


Displaying record number 565

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MAb ID 42F
HXB2 Location gp160(491-500)
DNA(7695..7724)
gp160 Epitope Map
Author Location gp120(491-500 HXB2)
Epitope IEPLGVAPTK Epitope Alignment
IEPLGVAPTK epitope logo
Subtype B
Ab Type gp120 C5
Neutralizing  
Species (Isotype) human(IgG1λ)
Patient  
Immunogen HIV-1 infection
Keywords ADCC, review

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Alsmadi1997 O. Alsmadi, R. Herz, E. Murphy, A. Pinter, and S. A. Tilley. A novel antibody-dependent cellular cytotoxicity epitope in gp120 is identified by two monoclonal antibodies isolated from a long-term survivor of human immunodeficiency virus type 1 infection. J. Virol., 71:925-33, 1997. PubMed ID: 8995609. Show all entries for this paper.

Alsmadi1998 O. Alsmadi and S. A. Tilley. Antibody-dependent cellular cytotoxicity directed against cells expressing human immunodeficiency virus type 1 Envelope of primary or laboratory-adapted strains by human and chimpanzee monoclonal antibodies of different epitope specificities. J. Virol., 72:286-93, 1998. PubMed ID: 9420226. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Pollara2013 Justin Pollara, Mattia Bonsignori, M. Anthony Moody, Marzena Pazgier, Barton F. Haynes, and Guido Ferrari. Epitope Specificity of Human Immunodeficiency Virus-1 Antibody Dependent Cellular Cytotoxicity (ADCC) Responses. Curr. HIV Res., 11(5):378-387, Jul 2013. PubMed ID: 24191939. Show all entries for this paper.


Displaying record number 740

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MAb ID 24G3
HXB2 Location gp160(525-543)
DNA(7797..7853)
gp160 Epitope Map
Author Location gp41(526-543 BH10)
Research Contact H. Katinger, Inst. Appl. Microbiol., Vienna, Austria
Epitope AAGSTMGAASMTLTVQARQ Epitope Alignment
AAGSTMGAASMTLTVQARQ epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1κ)
Patient  
Immunogen HIV-1 infection
Keywords  

Notes

Showing 2 of 2 notes.

References

Showing 3 of 3 references.

Isolation Paper
Buchacher1994 A. Buchacher, R. Predl, K. Strutzenberger, W. Steinfellner, A. Trkola, M. Purtscher, G. Gruber, C. Tauer, F. Steindl, A. Jungbauer, and H. Katinger. Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization. AIDS Res. Hum. Retroviruses, 10:359-369, 1994. A panel of 33 human monoclonal antibodies were produced. Linear epitopes for some of this set of MAbs were mapped using peptide ELISA. Linear epitopes were mapped in gp41, and a single epitope was mapped in p24. While multiple gp120 specific MAbs were generated, all seemed to be conformational or carbohydrate dependent, or both. PubMed ID: 7520721. Show all entries for this paper.

Buchacher1992 Andrea Buchacher, Renate Predl, Christa Tauer, Martin Purtscher, Gerhard Gruber, Renate Heider, Fraz Steindl, Alexandra Trkola, Alois Jungbauer, and Herman Katinger. Human Monoclonal Antibodies against gp41 and gp120 as Potential Agent for Passive Immunization. Vaccines, 92:191-195, 1992. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 741

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MAb ID 1A1
HXB2 Location gp160(525-543)
DNA(7797..7853)
gp160 Epitope Map
Author Location gp41(526-543 BH10)
Research Contact H. Katinger, Inst. Appl. Microbiol., Vienna, Austria
Epitope AAGSTMGAASMTLTVQARQ Epitope Alignment
AAGSTMGAASMTLTVQARQ epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1κ)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, antibody generation

Notes

Showing 3 of 3 notes.

References

Showing 2 of 2 references.

Isolation Paper
Buchacher1994 A. Buchacher, R. Predl, K. Strutzenberger, W. Steinfellner, A. Trkola, M. Purtscher, G. Gruber, C. Tauer, F. Steindl, A. Jungbauer, and H. Katinger. Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization. AIDS Res. Hum. Retroviruses, 10:359-369, 1994. A panel of 33 human monoclonal antibodies were produced. Linear epitopes for some of this set of MAbs were mapped using peptide ELISA. Linear epitopes were mapped in gp41, and a single epitope was mapped in p24. While multiple gp120 specific MAbs were generated, all seemed to be conformational or carbohydrate dependent, or both. PubMed ID: 7520721. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 739

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MAb ID 25C2 (IAM 41-25C2)
HXB2 Location gp160(525-543)
DNA(7797..7853)
gp160 Epitope Map
Author Location gp41(526-543 BH10)
Research Contact H. Katinger, Inst. Appl. Microbiol., Vienna, Austria and Viral Testing Systems, Houston, TX
Epitope AAGSTMGAASMTLTVQARQ Epitope Alignment
AAGSTMGAASMTLTVQARQ epitope logo
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1κ)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, antibody generation

Notes

Showing 3 of 3 notes.

References

Showing 4 of 4 references.

Isolation Paper
Buchacher1994 A. Buchacher, R. Predl, K. Strutzenberger, W. Steinfellner, A. Trkola, M. Purtscher, G. Gruber, C. Tauer, F. Steindl, A. Jungbauer, and H. Katinger. Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization. AIDS Res. Hum. Retroviruses, 10:359-369, 1994. A panel of 33 human monoclonal antibodies were produced. Linear epitopes for some of this set of MAbs were mapped using peptide ELISA. Linear epitopes were mapped in gp41, and a single epitope was mapped in p24. While multiple gp120 specific MAbs were generated, all seemed to be conformational or carbohydrate dependent, or both. PubMed ID: 7520721. Show all entries for this paper.

Buchacher1992 Andrea Buchacher, Renate Predl, Christa Tauer, Martin Purtscher, Gerhard Gruber, Renate Heider, Fraz Steindl, Alexandra Trkola, Alois Jungbauer, and Herman Katinger. Human Monoclonal Antibodies against gp41 and gp120 as Potential Agent for Passive Immunization. Vaccines, 92:191-195, 1992. Show all entries for this paper.

Sattentau1995 Q. J. Sattentau, S. Zolla-Pazner, and P. Poignard. Epitope Exposure on Functional, Oligomeric HIV-1 gp41 Molecules. Virology, 206:713-717, 1995. Most gp41 epitopes are masked when associated with gp120 on the cell surface. Weak binding of anti-gp41 MAbs can be enhanced by treatment with sCD4. MAb 2F5 binds to a membrane proximal epitope which binds in the presence of gp120 without sCD4. PubMed ID: 7530400. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 738

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MAb ID 5F3
HXB2 Location gp160(650-657)
DNA(8172..8195)
gp160 Epitope Map
Author Location gp160(650-657 BH10)
Research Contact H. Katinger, Inst. Appl. Microbiol., Vienna, Austria
Epitope QNQQEKNE Epitope Alignment
QNQQEKNE epitope logo
Ab Type  
Neutralizing  
Species (Isotype) human(IgG1λ)
Patient  
Immunogen HIV-1 infection
Keywords antibody binding site, antibody generation, antibody interactions, binding affinity, dendritic cells, genital and mucosal immunity, kinetics, neutralization

Notes

Showing 16 of 16 notes.

References

Showing 15 of 15 references.

Isolation Paper
Buchacher1994 A. Buchacher, R. Predl, K. Strutzenberger, W. Steinfellner, A. Trkola, M. Purtscher, G. Gruber, C. Tauer, F. Steindl, A. Jungbauer, and H. Katinger. Generation of Human Monoclonal Antibodies against HIV-1 Proteins; Electrofusion and Epstein-Barr Virus Transformation for Peripheral Blood Lymphocyte Immortalization. AIDS Res. Hum. Retroviruses, 10:359-369, 1994. A panel of 33 human monoclonal antibodies were produced. Linear epitopes for some of this set of MAbs were mapped using peptide ELISA. Linear epitopes were mapped in gp41, and a single epitope was mapped in p24. While multiple gp120 specific MAbs were generated, all seemed to be conformational or carbohydrate dependent, or both. PubMed ID: 7520721. Show all entries for this paper.

Chomont2008 Nicolas Chomont, Hakim Hocini, Jean-Chrysostome Gody, Hicham Bouhlal, Pierre Becquart, Corinne Krief-Bouillet, Michel Kazatchkine, and Laurent Bélec. Neutralizing Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Do Not Inhibit Viral Transcytosis Through Mucosal Epithelial Cells. Virology, 370(2):246-254, 20 Jan 2008. PubMed ID: 17920650. Show all entries for this paper.

Corti2010 Davide Corti, Johannes P. M. Langedijk, Andreas Hinz, Michael S. Seaman, Fabrizia Vanzetta, Blanca M. Fernandez-Rodriguez, Chiara Silacci, Debora Pinna, David Jarrossay, Sunita Balla-Jhagjhoorsingh, Betty Willems, Maria J. Zekveld, Hanna Dreja, Eithne O'Sullivan, Corinna Pade, Chloe Orkin, Simon A. Jeffs, David C. Montefiori, David Davis, Winfried Weissenhorn, Áine McKnight, Jonathan L. Heeney, Federica Sallusto, Quentin J. Sattentau, Robin A. Weiss, and Antonio Lanzavecchia. Analysis of Memory B Cell Responses and Isolation of Novel Monoclonal Antibodies with Neutralizing Breadth from HIV-1-Infected Individuals. PLoS One, 5(1):e8805, 2010. PubMed ID: 20098712. Show all entries for this paper.

Fiebig2009 Uwe Fiebig, Mirco Schmolke, Magdalena Eschricht, Reinhard Kurth, and Joachim Denner. Mode of Interaction between the HIV-1-Neutralizing Monoclonal Antibody 2F5 and Its Epitope. AIDS, 23(8):887-895, 15 May 2009. PubMed ID: 19414989. Show all entries for this paper.

Holl2006 Vincent Holl, Maryse Peressin, Thomas Decoville, Sylvie Schmidt, Susan Zolla-Pazner, Anne-Marie Aubertin, and Christiane Moog. Nonneutralizing Antibodies Are Able To Inhibit Human Immunodeficiency Virus Type 1 Replication in Macrophages and Immature Dendritic Cells. J. Virol., 80(12):6177-6181, Jun 2006. PubMed ID: 16731957. Show all entries for this paper.

Joyner2011 Amanda S. Joyner, Jordan R. Willis, James E.. Crowe, Jr., and Christopher Aiken. Maturation-Induced Cloaking of Neutralization Epitopes on HIV-1 Particles. PLoS Pathog., 7(9):e1002234, Sep 2011. PubMed ID: 21931551. Show all entries for this paper.

Kalia2005 Vandana Kalia, Surojit Sarkar, Phalguni Gupta, and Ronald C. Montelaro. Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41. J. Virol., 79(4):2097-2107, Feb 2005. PubMed ID: 15681412. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Peressin2011 M. Peressin, V. Holl, S. Schmidt, T. Decoville, D. Mirisky, A. Lederle, M. Delaporte, K. Xu, A. M. Aubertin, and C. Moog. HIV-1 Replication in Langerhans and Interstitial Dendritic Cells Is Inhibited by Neutralizing and Fc-Mediated Inhibitory Antibodies. J. Virol., 85(2):1077-1085, Jan 2011. PubMed ID: 21084491. Show all entries for this paper.

Perez2009 Lautaro G. Perez, Matthew R. Costa, Christopher A. Todd, Barton F. Haynes, and David C. Montefiori. Utilization of Immunoglobulin G Fc Receptors by Human Immunodeficiency Virus Type 1: A Specific Role for Antibodies against the Membrane-Proximal External Region of gp41. J. Virol., 83(15):7397-7410, Aug 2009. PubMed ID: 19458010. Show all entries for this paper.

Sheppard2007a Neil C. Sheppard, Sarah L. Davies, Simon A. Jeffs, Sueli M. Vieira, and Quentin J. Sattentau. Production and Characterization of High-Affinity Human Monoclonal Antibodies to Human Immunodeficiency Virus Type 1 Envelope Glycoproteins in a Mouse Model Expressing Human Immunoglobulins. Clin. Vaccine Immunol., 14(2):157-167, Feb 2007. PubMed ID: 17167037. Show all entries for this paper.

Vincent2008 Nadine Vincent, Amadou Kone, Blandine Chanut, Frédéric Lucht, Christian Genin, and Etienne Malvoisin. Antibodies Purified from Sera of HIV-1-Infected Patients by Affinity on the Heptad Repeat Region 1/Heptad Repeat Region 2 Complex of gp41 Neutralize HIV-1 Primary Isolates. AIDS, 22(16):2075-2085, 18 Oct 2008. PubMed ID: 18832871. Show all entries for this paper.

Vincent2012 Nadine Vincent and Etienne Malvoisin. Ability of Antibodies Specific to the HIV-1 Envelope Glycoprotein to Block the Fusion Inhibitor T20 in a Cell-Cell Fusion Assay. Immunobiology, 217(10):943-950, Oct 2012. PubMed ID: 22387075. Show all entries for this paper.

Ye2006 Ling Ye, Yuliang Sun, Jianguo Lin, Zhigao Bu, Qingyang Wu, Shibo Jiang, David A. Steinhauer, Richard W. Compans, and Chinglai Yang. Antigenic Properties of a Transport-Competent Influenza HA/HIV Env Chimeric Protein. Virology, 352(1):74-85, 15 Aug 2006. PubMed ID: 16725170. Show all entries for this paper.

Yuan2009 Wen Yuan, Xing Li, Marta Kasterka, Miroslaw K. Gorny, Susan Zolla-Pazner, and Joseph Sodroski. Oligomer-Specific Conformations of the Human Immunodeficiency Virus (HIV-1) gp41 Envelope Glycoprotein Ectodomain Recognized by Human Monoclonal Antibodies. AIDS Res. Hum. Retroviruses, 25(3):319-328, Mar 2009. PubMed ID: 19292593. Show all entries for this paper.


Displaying record number 914

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MAb ID AM5C6
HXB2 Location Nef(28-43 + 82-92)
DNA(8878..8925,9040..9072)
Nef Epitope Map
Author Location Nef(28-43 BH10)
Epitope DGVGAASRDLEKHGAI + KAAVDLSHFLK (Discontinuous epitope) Epitope Alignment
DGVGAASRDLEKHGAI + KAAVDLSHFLK epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Nef

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Schneider1991 T. Schneider, H.-P. Harthus, P. Heldebrandt, M. Niedrig, M. Broker, W. Weigelt, A. Beck, and G. Pauli. Epitopes of the HIV-1-Negative Factor Reactive with Murine Monoclonal Antibodies and Human Hiv-1-Positive Sera. AIDS Res. Hum. Retroviruses, 7:37-43, 1991. Epitopes for 9 murine MAbs were mapped, and found to be located in 4 immunogenic regions. 7/10 sera from HIV-1 positive individuals reacted to the four nef immunogenic regions. PubMed ID: 1707640. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 915

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MAb ID 26/76
HXB2 Location Nef(30-43)
DNA(8884..8925)
Nef Epitope Map
Author Location Nef(30-43 BH10)
Epitope VGAASRDLEKHGAI Epitope Alignment
VGAASRDLEKHGAI epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Nef

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Schneider1991 T. Schneider, H.-P. Harthus, P. Heldebrandt, M. Niedrig, M. Broker, W. Weigelt, A. Beck, and G. Pauli. Epitopes of the HIV-1-Negative Factor Reactive with Murine Monoclonal Antibodies and Human Hiv-1-Positive Sera. AIDS Res. Hum. Retroviruses, 7:37-43, 1991. Epitopes for 9 murine MAbs were mapped, and found to be located in 4 immunogenic regions. 7/10 sera from HIV-1 positive individuals reacted to the four nef immunogenic regions. PubMed ID: 1707640. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 916

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MAb ID 25/03
HXB2 Location Nef(30-43)
DNA(8884..8925)
Nef Epitope Map
Author Location Nef(30-43 BH10)
Epitope VGAASRDLEKHGAI Epitope Alignment
VGAASRDLEKHGAI epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Nef

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Schneider1991 T. Schneider, H.-P. Harthus, P. Heldebrandt, M. Niedrig, M. Broker, W. Weigelt, A. Beck, and G. Pauli. Epitopes of the HIV-1-Negative Factor Reactive with Murine Monoclonal Antibodies and Human Hiv-1-Positive Sera. AIDS Res. Hum. Retroviruses, 7:37-43, 1991. Epitopes for 9 murine MAbs were mapped, and found to be located in 4 immunogenic regions. 7/10 sera from HIV-1 positive individuals reacted to the four nef immunogenic regions. PubMed ID: 1707640. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 917

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MAb ID 3F2
HXB2 Location Nef(31-40)
DNA(8887..8916)
Nef Epitope Map
Author Location Nef(31-40 BRU)
Epitope GAASRDLEKH Epitope Alignment
GAASRDLEKH epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BRU
Vaccine component Nef

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Ovod1992 V. Ovod, A. Lagerstedt, A. Ranki, F. O. Gombert, R. Spohn, M. Tahtinen, G. Jung, and K. J. Krohn. Immunological Variation and Immunohistochemical Localization of HIV-1 Nef Demonstrated with Monoclonal Antibodies. AIDS, 6:25-34, 1992. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 1371924. Show all entries for this paper.

Saito1994 Y. Saito, L. Sharer, L. Epstein, and et. al. Overexpression of Nef as a Marker for Restricted HIV-1 Infection of Astrocytes in Postmortem Pediatric Central Nervous Tissues. Neurology, 44:474-481, 1994. PubMed ID: 8145918. Show all entries for this paper.

Ranki1995 A. Ranki, M. Nyberg, V. Ovod, M. Haltia, I. Elovaara, R. Raininko, H. Haapasalo, and K. Krohn. Abundant Expression of HIV Nef and Rev Proteins in Brain Astrocytes In Vivo Is Associated with Dementia. AIDS, 9:1001-1008, 1995. HIV Nef protein was found in the brain cells of infected individuals with clinical neurological disease. PubMed ID: 8527071. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 918

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MAb ID 3D12
HXB2 Location Nef(31-50)
DNA(8887..8946)
Nef Epitope Map
Author Location Nef(31-50 BRU)
Epitope GAASRDLEKHGAITSSNTAA Epitope Alignment
GAASRDLEKHGAITSSNTAA epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BRU
Vaccine component Nef

Notes

Showing 6 of 6 notes.

References

Showing 4 of 4 references.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Ovod1992 V. Ovod, A. Lagerstedt, A. Ranki, F. O. Gombert, R. Spohn, M. Tahtinen, G. Jung, and K. J. Krohn. Immunological Variation and Immunohistochemical Localization of HIV-1 Nef Demonstrated with Monoclonal Antibodies. AIDS, 6:25-34, 1992. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 1371924. Show all entries for this paper.

Ranki1995 A. Ranki, M. Nyberg, V. Ovod, M. Haltia, I. Elovaara, R. Raininko, H. Haapasalo, and K. Krohn. Abundant Expression of HIV Nef and Rev Proteins in Brain Astrocytes In Vivo Is Associated with Dementia. AIDS, 9:1001-1008, 1995. HIV Nef protein was found in the brain cells of infected individuals with clinical neurological disease. PubMed ID: 8527071. Show all entries for this paper.

Saito1994 Y. Saito, L. Sharer, L. Epstein, and et. al. Overexpression of Nef as a Marker for Restricted HIV-1 Infection of Astrocytes in Postmortem Pediatric Central Nervous Tissues. Neurology, 44:474-481, 1994. PubMed ID: 8145918. Show all entries for this paper.


Displaying record number 1031

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MAb ID polyclonal
HXB2 Location Nef(33-65)
DNA(8893..8991)
Nef Epitope Map
Author Location Nef(32-64 LAI, BRU)
Epitope ASRDLEKHGAITSSNTAATNAACAWLEAQEEEE Epitope Alignment
Epitope Name PF13
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen HIV-1 infection, vaccine
Keywords  

Vaccine Details

Vaccine type protein, PLG microparticle
Vaccine strain B clade BRU, B clade LAI
Vaccine component Nef
Adjuvant Complete Freund's Adjuvant (CFA), PLG

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Moureau2002 Corinne Moureau, Pierre-Louis Vidal, Yamina Bennasser, Marinette Moynier, Yvan Nicaise, Muriel Aussillous, Sophie Barthelemy, Luc Montagnier, and Elmostafa Bahraoui. Characterization of Humoral and Cellular Immune Responses in Mice Induced by Immunization with HIV-1 Nef Regulatory Protein Encapsulated In Poly(DL-Lactide-Co-Glycolide) Microparticles. Mol. Immunol., 38(8):607-618, Jan 2002. PubMed ID: 11792429. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 1032

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MAb ID polyclonal
HXB2 Location Nef(119-168)
DNA(9151..9300)
Nef Epitope Map
Author Location Nef(118-167 LAI, BRU)
Epitope GYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPV Epitope Alignment
Epitope Name PF15
Subtype B
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen HIV-1 infection, vaccine
Keywords  

Vaccine Details

Vaccine type protein, PLG microparticle
Vaccine strain B clade BRU, B clade LAI
Vaccine component Nef
Adjuvant Complete Freund's Adjuvant (CFA), PLG

Notes

Showing 2 of 2 notes.

References

Showing 2 of 2 references.

Moureau2002 Corinne Moureau, Pierre-Louis Vidal, Yamina Bennasser, Marinette Moynier, Yvan Nicaise, Muriel Aussillous, Sophie Barthelemy, Luc Montagnier, and Elmostafa Bahraoui. Characterization of Humoral and Cellular Immune Responses in Mice Induced by Immunization with HIV-1 Nef Regulatory Protein Encapsulated In Poly(DL-Lactide-Co-Glycolide) Microparticles. Mol. Immunol., 38(8):607-618, Jan 2002. PubMed ID: 11792429. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 926

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MAb ID 2F2
HXB2 Location Nef(151-170)
DNA(9247..9306)
Nef Epitope Map
Author Location Nef(151-170 BRU)
Epitope DKVEEANKGENTSLLHPVSL Epitope Alignment
DKVEEANKGENTSLLHPVSL epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine component Nef

Notes

Showing 6 of 6 notes.

References

Showing 4 of 4 references.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.

Ovod1992 V. Ovod, A. Lagerstedt, A. Ranki, F. O. Gombert, R. Spohn, M. Tahtinen, G. Jung, and K. J. Krohn. Immunological Variation and Immunohistochemical Localization of HIV-1 Nef Demonstrated with Monoclonal Antibodies. AIDS, 6:25-34, 1992. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 1371924. Show all entries for this paper.

Ranki1995 A. Ranki, M. Nyberg, V. Ovod, M. Haltia, I. Elovaara, R. Raininko, H. Haapasalo, and K. Krohn. Abundant Expression of HIV Nef and Rev Proteins in Brain Astrocytes In Vivo Is Associated with Dementia. AIDS, 9:1001-1008, 1995. HIV Nef protein was found in the brain cells of infected individuals with clinical neurological disease. PubMed ID: 8527071. Show all entries for this paper.

Saito1994 Y. Saito, L. Sharer, L. Epstein, and et. al. Overexpression of Nef as a Marker for Restricted HIV-1 Infection of Astrocytes in Postmortem Pediatric Central Nervous Tissues. Neurology, 44:474-481, 1994. PubMed ID: 8145918. Show all entries for this paper.


Displaying record number 927

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MAb ID E9
HXB2 Location Nef(158-181)
DNA(9268..9339)
Nef Epitope Map
Author Location Nef(158-206 IIIB)
Epitope KGENTSLLHPVSLHGMDDPEREVL Epitope Alignment
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgM)
Patient  
Immunogen  
Keywords  

Notes

Showing 4 of 4 notes.

References

Showing 5 of 5 references.

Fujii1993 Y. Fujii, Y. Nishino, T. Nakaya, K. Tokunaga, and K. Ikuta. Expression of Human Immunodeficiency Virus Type 1 Nef Antigen on the Surface of Acutely and Persistently Infected Human T-cells. Vaccine, 11:1240, 1993. PubMed ID: 8256505. Show all entries for this paper.

Otake1994 K. Otake, Y. Fujii, Y. Nishino, Q. Zhong, K. Fujinaga, M. Kameoka, K. Ohki, and K. Ikuta. The Carboxyl-Terminal Region of HIV-1 Nef Protein Is a Cell Surface Domain That Can Interact with CD4+ T Cells. J. Immunol., 153:5826-5837, 1994. This study shows that the C-terminal end of Nef is accessible to Abs. This domain could bind in a soluble form to CD4+, uninfected cells, and this interaction is inhibited in the presence of the C-terminal specific antibodies. Syncytium formation was reduced by these Abs or peptides. Abs could stain IIIB/M10, but not MN/M10, infected cells, in a membrane immunofluorescence assay. PubMed ID: 7989778. Show all entries for this paper.

Fujii1996 Y. Fujii, K. Otake, M. Tashiro, and A. Adachi. In Vitro Cytocidal Effects of Human Immunodeficiency Virus Type 1 Nef on Unprimed Human CD4+ T Cells without MHC Restriction. J. Gen. Virol., 77:2943-2951, 1996. PubMed ID: 9000084. Show all entries for this paper.

Fujii1996b Y. Fujii, K. Otake, M. Tashiro, and A. Adachi. Human Immunodeficiency Type 1 Nef Protein on the Cell Surface Is Cytocidal for Human CD4+ T cells. FEBS Lett., 393:105-108, 1996. PubMed ID: 8804435. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


Displaying record number 928

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MAb ID 3E6
HXB2 Location Nef(161-180)
DNA(9277..9336)
Nef Epitope Map
Author Location Nef(161-180 BRU)
Epitope NTSLLHPVSLHGMDDPEREV Epitope Alignment
NTSLLHPVSLHGMDDPEREV epitope logo
Ab Type  
Neutralizing  
Species (Isotype) mouse(IgG1)
Patient  
Immunogen vaccine
Keywords  

Vaccine Details

Vaccine type protein
Vaccine strain B clade BRU
Vaccine component Nef

Notes

Showing 4 of 4 notes.

References

Showing 4 of 4 references.

Ovod1992 V. Ovod, A. Lagerstedt, A. Ranki, F. O. Gombert, R. Spohn, M. Tahtinen, G. Jung, and K. J. Krohn. Immunological Variation and Immunohistochemical Localization of HIV-1 Nef Demonstrated with Monoclonal Antibodies. AIDS, 6:25-34, 1992. Ten anti-Nef MAbs were generated and mapped. Nef is expressed in two isomorphic forms, and was shown to be expressed mainly in the Golgi complex and at the nuclear membrane, but occasionally x in the nucleus, particularly in MT-4 cells. PubMed ID: 1371924. Show all entries for this paper.

Saito1994 Y. Saito, L. Sharer, L. Epstein, and et. al. Overexpression of Nef as a Marker for Restricted HIV-1 Infection of Astrocytes in Postmortem Pediatric Central Nervous Tissues. Neurology, 44:474-481, 1994. PubMed ID: 8145918. Show all entries for this paper.

Ranki1995 A. Ranki, M. Nyberg, V. Ovod, M. Haltia, I. Elovaara, R. Raininko, H. Haapasalo, and K. Krohn. Abundant Expression of HIV Nef and Rev Proteins in Brain Astrocytes In Vivo Is Associated with Dementia. AIDS, 9:1001-1008, 1995. HIV Nef protein was found in the brain cells of infected individuals with clinical neurological disease. PubMed ID: 8527071. Show all entries for this paper.

Maksiutov2002 A. Z. Maksiutov, A. G. Bachinskii, and S. I. Bazhan. [Searching for Local Similarities Between HIV-1 and Human Proteins. Application to Vaccines]. Mol Biol (Mosk), 36(3):447-459, May-Jun 2002. Article in Russian. PubMed ID: 12068630. Show all entries for this paper.


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