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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

Showing 2 of 2 notes.

12G-A8g2: This epitope is similar to a fragment of the human protein CD40 ligand TNF-related activation protein (T-cell antigen GP39)(CD154), LDKIEDERN, as well as to a fragment of Lens-epithelium-derived growth factor, DIITEEDKSKKKGQ. Maksiutov2002
12G-A8g2: Bound to 30-mer, but not to internal peptides -- did not bind live infected cells -- antigenic domain known as HPG30. Shang1991

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.

12I-D12g2: This epitope is similar to a fragment of the human protein CD40 ligand TNF-related activation protein (T-cell antigen GP39) (CD154), LDKIEDERN, as well as to a fragment of Lens-epithelium-derived growth factor, DIITEEDKSKKKGQ. Maksiutov2002
12I-D12g2: Bound to 30-mer, but not to internal peptides -- did not bind live infected cells -- antigenic domain known as HPG30. Shang1991

References

Showing 2 of 2 references.

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.

12G-H1c7: This epitope is similar to a fragment of the human protein CD40 ligand TNF-related activation protein (T-cell antigen GP39) (CD154), LDKIEDERN, as well as to a fragment of Lens-epithelium-derived growth factor, DIITEEDKSKKKGQ. Maksiutov2002
12G-H1c7: Bound to 30-mer, but not to internal peptides -- did not bind live infected cells -- antigenic domain known as HPG30. Shang1991

References

Showing 2 of 2 references.

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.

12G-D7h11: This epitope is similar to a fragment of the human protein CD40 ligand TNF-related activation protein (T-cell antigen GP39) (CD154), LDKIEDERN, as well as to a fragment of Lens-epithelium-derived growth factor, DIITEEDKSKKKGQ. Maksiutov2002
12G-D7h11: Bound to 30-mer, but not to internal peptides -- did not bind live infected cells -- antigenic domain known as HPG30. Shang1991

References

Showing 2 of 2 references.

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
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.

11H9: UK Medical Research Council AIDS reagent: ARP344.
11H9: This epitope is similar to a fragment of Lens-epithelium-derived growth factor, DIITEEDKSKKKGQ. Maksiutov2002
11H9: Reactive against p18 and p55. Ferns1987

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.

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
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.

anti-K159: This epitope is similar to a fragment of the human protein Apoptosis regulator BCL-W (KIAA0271), ESVNKEMEPLVGQV. Maksiutov2002
anti-K159: Both the peptide K159, SQGVVESMNKELKKIIGQVRDQAEHLKTA, and the Abs raised against this peptide inhibit Integrase activity -- K159 was found to fulfill condition of minimal number of helical heptads to achieve the formation of a stable coiled-coil structure -- Integrase is proposed to function as a dimer interacting in this region. Maroun1999

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.

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
Ab Type
Neutralizing
Species (Isotype)
Patient
Immunogen
Keywords

Notes

Showing 2 of 2 notes.

10.1: This epitope is similar to a fragment of the human protein Complement 4 (containing C4A anaphlylatoxin), GRRNRRRR. Maksiutov2002
10.1: Binds to the RRE binding site -- polyclonal anti-Rev Ab detected Rev in astrocytes in 4/5 brain autopsy samples, but only one of these was positive using 10.1, suggesting most Rev was bound to RRE. Ranki1995

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.

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
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.

3H6: This epitope is similar to a fragment of the human protein Complement 4 (containing C4A anaphlylatoxin), GRRNRRRR. Maksiutov2002
3H6: Directed against nucleolar localization/RRE binding domain -- antigenic domain tentative, MAb failed to bind a RRNRRR Rev deletion mutant. Orsini1995 (antibody generation)
3H6 database comment: There is another MAb with this ID that recognizes gp41.

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.

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
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.

8E7: This epitope is similar fragments of the human protein Epidermal growth factor receptor substrate 15, EPVPMSLPPA, and Insulin-like growth factor binding protein complex acid labile chain precursor, QPPGLERLWLEGNPWDCG. Maksiutov2002
8E7: HIV-1 RNA and Rev localize to the same region in the nucleoplasm, but the splicing factor SC-35 localizes in different speckles with the nucleoplasm than Rev -- intron containing beta-globin was distributed similarly to HIV-1, suggesting Rev and HIV-1 RNAs interact at putative sites of mRNA transcriptions and splicing. Boe1998
8E7: Peptide interaction mapped to aa 70-84, 75-88 -- protein footprint to 65-88. Jensen1997
8E7: 8E7 worked in indirect immunofluorescence and also detected Rev in WB assays -- used to detect localization of Rev in several compartments including the nucleoli, nucleoplasm, perinuclear zone, and cytoplasm -- Rev co-localized with host cell factors known to assemble on nascent transcripts -- Rev shuttles continuously between cytoplasmic and nucleoplasmic compartments. Kalland1994,Kalland1994a,Szilvay1995

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.

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
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.

9G2: Called 9G2G4D6E8: UK Medical Research Council AIDS reagent: ARP3058.
9G2: This epitope is similar fragments of the human protein Epidermal growth factor receptor substrate 15, EPVPMSLPPA, and Insulin-like growth factor binding protein complex acid labile chain precursor, QPPGLERLWLEGNPWDCG. Maksiutov2002
9G2: Peptide interaction mapped to aa 70-84, 75-88 -- protein footprint to 65-88. Jensen1997
9G2: Worked in indirect immunofluorescence and also detected Rev in WB assays -- used to detect localization of Rev throughout the cell. Kalland1994

References

Showing 3 of 3 references.

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
Ab Type
Neutralizing
Species (Isotype)	(IgG1)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine component	Rev

Notes

Showing 2 of 2 notes.

Ab4: This epitope is similar fragments of the human protein Epidermal growth factor receptor substrate 15, EPVPMSLPPA, and Insulin-like growth factor binding protein complex acid labile chain precursor, QPPGLERLWLEGNPWDCG. Maksiutov2002
Ab4: The binding site overlaps the nuclear export signal -- binding was not blocked by bound HIV RNA and may be accessible for protein interaction. Henderson1997

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.

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
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.

7E2/4: UK Medical Research Council AIDS reagent: ARP3050.
7E2/4: This epitope has a high degree of similarity with the platelet membrane glycoprotein IIIA precursor (GLIIIA) (integrin beta- 3) (CD61): PLYKEATSTF. Maksiutov2002
7E2/4: C1 domain -- the relative affinity for denatured/native gp120 is .07, suggesting conformational component. Moore1994a

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.

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
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.

4D4#85: Similarity level of the 4D4#85 binding site pentapeptide VPVWK to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 1 time, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome. Kanduc2008 (immunotherapy)
4D4#85: This epitope has a high degree of similarity with the platelet membrane glycoprotein IIIA precursor (GLIIIA) (integrin beta- 3) (CD61): PLYKEATSTF. Maksiutov2002 (antibody polyreactivity)
4D4#85: A panel of MAbs were shown to bind with similar or greater affinity and similar competition profiles to a deglycosylated or variable loop deleted core gp120 protein (Delta V1, V2, and V3), thus such a core protein produces a structure closely approximating full length folded monomer. Binley1998
4D4#85: Binds efficiently to sgp120 but not soluble gp120+gp41, suggesting its gp120 epitope is blocked by gp41 binding -- does not bind to HXBc2 gp120 if the 19 C-term amino acids, in conjunction with C1 positions 31-50, are deleted. Wyatt1997
4D4#85: Inhibits binding of C1 MAb M85, C1-C5 discontinuous epitope MAbs 181 and 212A, and CD4 binding induced MAbs 48d and 17b. Moore1996
4D4#85: C1 domain -- the relative affinity, denatured/native gp120 is 0.1 -- mutation 45 W/S impairs binding. Moore1994a

References

Showing 7 of 7 references.

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.

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
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.

M92: This epitope has a high degree of similarity with the platelet membrane glycoprotein IIIA precursor (GLIIIA) (integrin beta- 3) (CD61): PLYKEATSTF. Maksiutov2002
M92: The relative affinity for denatured/native gp120 is 1. Moore1994a
M92: Immunoblot reactive, RIP negative, but precipitates deglycosylated gp120 -- reacts with strains IIIB, 451, MN, RF, and RUTZ. Veronese1992

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.

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
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.

M86: This epitope has a high degree of similarity with the platelet membrane glycoprotein IIIA precursor (GLIIIA) (integrin beta- 3) (CD61): PLYKEATSTF. Maksiutov2002
M86: C1 domain -- the relative affinity for denatured/native gp120 is 1. Moore1994a
M86: Immunoblot and RIP reactive for strains IIIB, 451, MN, RF, and RUTZ -- binds deglycosylated gp120. Veronese1992

References

Showing 3 of 3 references.

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
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.

697-D: The authors selected an optimal panel of diverse HIV-1 envelope glycoproteins to represent the antigenic diversity of HIV globally in order to be used as antigen candidates. The selection was based on genetic and geographic diversity, and experimentally and computationally evaluated humoral responses. The eligibility of the envelopes as vaccine candidates was evaluated against a panel of antibodies for breadth, affinity, binding and durability of vaccine-elicited responses. The antigen panel was capable of detecting the spectrum of V2-specific antibodies that target epitopes from the V2 strand C (V2p), the integrin binding motif in V2 (V2i), and the quaternary epitope at the apex of the trimer (V2q). Yates2018 (vaccine antigen design, vaccine-induced immune responses, binding affinity)
697-D: To understand HIV neutralization mediated by the MPER, antibodies and viruses were studied from CAP206, a patient known to produce MPER-targeted neutralizing mAbs. 41 human mAbs were isolated from CAP206 at various timepoints after infection, and 4 macaque mAbs were isolated from animals immunized with CAP206 Env proteins. Two rare, naturally-occuring single-residue changes in Env were identified in transmitted/founder viruses (W680G in CAP206 T/F and Y681D in CH505 T/F) that made the viruses less resistant to neutralization. The results point to the role of the MPER in mediating the closed trimer state, and hence the neutralization resistance of HIV. CH58 was one of several mAbs tested for neutralization of transmitted founder viruses isolated from clade C infected individuals CAP206 and CH505, compared to T/F viruses containing MPER mutations that confer enhanced neutralization sensitivity. Bradley2016a (neutralization)
697-D: The study compared various factors affecting the accessibility of epitopes for antibodies targeting the V2 integrin (V2i) region, versus the V3 region. CD4 treament of BaL and JRFL pseudoviruses increased their neutralization sensitivity to V3 MAbs, but not to V2i MAbs. Viruses grown in a glycosidase inhibitor were more sensitive to neutralization by V3, but not V2i, MAbs. Increasing the time of virus-MAb interaction increased virus neutralization by some V2i MAbs and all V3 MAbs. The structural dynamics of V2i and V3 epitopes has important effects in neutralization. The V2i MAbs tested were: 697, 830A, 1357, 1361, 1393, 2158, and 2297. Upadhyay2014 (glycosylation, neutralization)
697-3D: The infectious virion (iVirions) capture index (IVCI) of different Abs have been determined. bnAbs captured higher proportions of iVirions compared to total virus particles (rVirions) indicating the capacity, breadth and selectively of bnAbs to capture iVirions. IVCI was additive with a mixture of Abs, providing proof of concept for vaccine-induced effect of improved capacity. MAb 697-30D showed 20% capacity. Liu2014 (binding affinity)
697-D: Four V2 MAbs CH58, CH59, HG107 and HG120 were isolated from RV144 Thai HIV-1 vaccinees. These MAbs recognized residue 169, neutralized laboratory HIV-1 (tier 1 strains) and mediated ADCC. 697D was used in the study as a V2 conformational mAb control to study the binding of the new mAb isolates. Liao2013b (ADCC)
697-D: This study characterized the Elisa cross-reactivity, neutralization, and Ig variable genes of a panel of 7 anti-V2 mAbs: 1361, 1393A, 1357, 697, 830A, 2158, and 2297. Despite sequence variability, the 7 mAbs recognize conserved immunologic features of V2, with 6 of them targeting similar epitopes. The crystal structure of the mAb 697 binding site was determined. Gorny2012 (neutralization, structure)
697-D: This study analyzed the neutralization sensitivity of sequential HIV-1 primary isolates during their natural evolution in 5 subtype B and CRF02_AG HIV-1 infected drug naive individuals to 13 anti-HIV-1 MAbs (including this MAb) directed at epitopes in the V2, V3, CD4bd and carbohydrates. Patient viruses evolved to become more sensitive to neutralization by MAbs directed at epitopes at V2, V3 and CDbd, indicating that cross sectional studies are inadequate to define the neutralization spectrum of MAb neutralization with primary HIV-1 isolates. Haldar2011 (neutralization)
697-D: gp120 in complex with 697-D had higher reactivity with 694/98-D compared to the uncomplexed gp120. Hioe2009 (binding affinity)
697-D: This review summarizes 697-D Ab epitope, properties and neutralization activity. Kramer2007 (review)
697-D: The study evaluated the influence of glycosylation within the V1/V2 domain on antibody recognition. Recombinant proteins, demonstrated to be folded in native conformation, were produced following transfection of CHO cells by plasmids expressing V1/V2 domains from primary isolates of different clades. This Ab was used to validate the functional structure of the recombinant proteins produced. Granados-Gonzalez2008
697-D: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alternations of both gp41 and gp120. The alternations did not affect virus CD4 binding, coreceptor binding site exposure, or infectivity of the virus, but did result in decreased binding and neutralization by certain MAbs and human sera. 697-30D showed a decrease in binding to the LLP-2 mutant compared to the wildtype virus, indicating that its epitope was altered by the mutation. Kalia2005 (antibody binding site, binding affinity)
697-D: This review focuses on the importance of neutralizing Abs in protecting against HIV-1 infection, including mechanisms of Ab interference with the viral lifecycle, Ab responses elicited during natural HIV infection, and use of monoclonal and polyclonal Abs in passive immunization. In addition, vaccine design strategies for eliciting of protective broadly neutralizing Abs are discussed. MAbs included in this review are: 2F5, Clone 3 (CL3), 4E10, Z13, IgG1b12, 2G12, m14, 447-52D, 17b, X5, m16, 47e, 412d, E51, CM51, F105, F425, 19b, 2182, DO142-10, 697-D, 448D, 15e and Cβ1. McCann2005 (antibody binding site, review)
697-D: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
697-D: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. V2 MAb 697-D did not bind to mCHO and had diminished binding to GDMR, while V2 MAb 8.22.2 bound to GDMR but not mCHO. Selvarajah2005 (vaccine antigen design, vaccine-induced immune responses)
697-D: In a review of Envelope binding MAbs in this database, V2-specific MAbs are noted to have some ability to neutralize HIV-1, but generally weak with limited cross-reactivity; it weakly neutralizes some primary but not TCLA strains. 697-D is the best characterized of the anti-V2 MAbs, and binds weakly and sporadically to isolates from clades A-D. Gorny2003 (variant cross-reactivity, review, subtype comparisons)
697-D: This epitope is similar to a fragment of the human protein macrophage colony stimulating factor I receptor SISIRLKVQK. Maksiutov2002
697-D: Called 697D -- Transgenic mice carrying human genes allowing production of fully human MAbs were used to rapidly create a panel of anti-HIV gp120 MAb producing hybridomas by immunization with HIV SF162 gp120 -- the previously described human MAbs 5145A, 4117C and 697D were used as controls. He2002
697-D: Called 697D -- Truncation of the gp41 cytoplasmic domain of X4, R5, and X4R5 viruses forces a conformation that more closely resembles the CD4 bound state of the external Envelope, enhancing binding of CD4i MAbs 17b and 48d and of CD4BS MAbs F105, b12, and in most cases of glycosylation site dependent MAb 2G12 and the anti-gp41 MAb 246D -- in contrast, binding of the anti-V2 MAb 697D and the anti-V3 MAb 694/98D were not affected -- viruses bearing the truncation were more sensitive to neutralization by MAbs 48d, b12, and 2G12 -- the anti-C5 MAb 1331A was used to track levels of cell surface expression of the mutated proteins. EdwardsBH2002 (antibody binding site)
697-D: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 5 anti-V2 MAbs, which showed weak and sporadic binding, with the most frequent binding to C and D clades. Nyambi2000 (subtype comparisons)
697-D: Ab responses, because of their capacity to alter antigen uptake and processing, can influence helper T cell responses -- CD4BS MAbs or serum Ig from HIV+ individuals inhibited proliferative responses of gp120 specific T cells -- V2 MAb 697-D did not affect proliferation. Hioe2000
697-D: Binding of panel of 21 MAbs to soluble oligomeric gp140 versus gp41 or gp120 monomers was compared -- no MAb was oligomer specific, though anti-V3 and CD4BS MAbs reacted better with the oligomer and V2 and C5 tended to favor the monomer -- V2 MAbs 697-D, 1357 and 1361 favored the monomer by approximately 2 fold. Gorny2000b (antibody binding site)
697-D: Called 697-30D -- deleting the V2 loop of neutralization-resistant HIV-1 isolate SF162 does not abrogate its replication in PBMC or macrophages, but it enhances its neutralization sensitivity to sera from patients with B clade infection up to 170-fold, and also enhances sensitivity to sera from clades A through F -- deletion of V1 or V2 did not enable neutralization by V2 MAbs G3.4, G3.136, or 687-30D. Stamatatos1998 (variant cross-reactivity)
697-D: Using a whole virion-ELISA method, 18 human MAbs were tested for their ability to bind to a panel of 9 viruses from clades A, B, D, F, G, and H -- V2 Abs 697-D, 1361, and 1357 tended to bind weakly with a similar pattern of specificity to virions, and bound well to soluble gp120: weak binding to 1/4 B clade viruses (CA5), and weak binding to viruses from subtype A and D. Nyambi1998 (subtype comparisons)
697-D: Does not neutralize TCLA strains but neutralizes some primary isolates weakly. Parren1997 (variant cross-reactivity)
697-D: Study shows neutralization is not predicted by MAb binding to JRFL monomeric gp120, but is associated with oligomeric Env binding -- 697-D bound monomer, did not bind oligomer or neutralize JRFL. Fouts1997 (antibody binding site)
697-D: Partial inhibition of gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study. Trkola1996b (co-receptor)
697-D: Review: called 697/30D -- neutralizes some primary, but not lab adapted strains. Moore1995c (variant cross-reactivity, review)
697-D: Not neutralizing, no ADCC activity, and no viral enhancing activity. Forthal1995 (enhancing activity)
697-D: Conformational with weak reactivity to V2 peptide ISTSIRGKVQKEYAFFYKLD -- neutralized 3/4 primary isolates, but none of 4 lab strains -- V2 substitutions 176/177 FY/AT, 179/180 LD/DL, 183/184 PI/SG, and 192-194 YSL/GSS abrogate binding -- anti-C4 MAbs G3-536 and G45-60 enhance binding -- mild oxidation of carbohydrate moieties inhibits binding. Gorny1994 (antibody binding site, antibody generation)

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.

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

Download this epitope record as JSON.

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
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.

8.22.2: The study evaluated the influence of glycosylation within the V1/V2 domain on antibody recognition. Recombinant proteins, demonstrated to be folded in native conformation, were produced following transfection of CHO cells by plasmids expressing V1/V2 domains from primary isolates of different clades. This Ab was used to validate the functional structure of the recombinant proteins produced. Granados-Gonzalez2008
8.22.2: This Ab was used to help define the antigenic profile of envelopes used in serum depletion experiments to attempt to define the neutralizing specificities of broadly cross-reactive neutralizing serum. This Ab bound to JR-FL and JR-CSF gp120 monomers but not to core JR-CSF gp120 monomer used in the same experiments. V1, V2, and V3 specificities did not contribute to the broadly neutralizing capability of sera from 3 (2 B clade ,1 A clade) HIV infected individuals. Dhillon2007 (antibody binding site, neutralization)
8.22.2: Antigens were designed to attempt to target immune responses toward the IgG1b12 epitope, while minimizing antibody responses to less desirable epitopes. One construct had a series of substitutions near the CD4 binding site (GDMR), the other had 7 additional glycans (mCHO). The 2 constructs did not elicit b12-like neutralizing antibodies, but both antigens successfully dampened other responses that were intended to be dampened while not obscuring b12 binding. V2 MAb 697-D did not bind to mCHO and had diminished binding to GDMR, while V2 MAb 8.22.2 bound to GDMR but not mCHO. Selvarajah2005 (vaccine antigen design, vaccine-induced immune responses)
8.22.2: By adding N-linked glycosylation sites to gp120, epitope masking of non-neutralizing epitopes can be achieved leaving the IgG1b12 binding site intact. This concept was originally tested with the addition of four glycosylation sites, but binding to b12 was reduced. It was modified here to exclude the C1 N-terminal region, and to include only three additional glycosylation sites. This modified protein retains full b12 binding affinity and it masks other potentially competing epitopes, and does not bind to 21 other MAbs to 7 epitopes on gp120, including 8.22.2. Pantophlet2004 (vaccine antigen design)
8.22.2: V1V2 was determined to be the region that conferred the neutralization phenotype differences between two R5-tropic primary HIV-1 isolates, JRFL and SF162. JRFL is resistant to neutralization by many sera and MAbs, while SF162 is sensitive. All MAbs tested, anti-V3, -V2, -CD4BS, and -CD4i, (except the broadly neutralizing MAbs IgG1b12, 2F5, and 2G12, which neutralized both strains), neutralized the SF162 pseudotype but not JRFL, and chimeras that exchanged the V1V2 loops transferred the neutralization phenotype. Three anti-V2 MAb were tested -- 8.22.2 weakly neutralized SF162, and did not neutralize JRFL at all. Pinter2004 (variant cross-reactivity)
8.22.2: This broad review of anti-Envelope MAbs notes that V2 MAbs are generally weakly neutralizing at best, and somewhat strain specific. 8.22.2 weakly neutralizes SF162. Gorny2003 (review)
8.22.2: This epitope is similar to a fragment of the human protein macrophage colony stimulating factor I receptor SISIRLKVQK. Maksiutov2002
8.22.2 : Transgenic mice (strain XenoMouse G2) carrying human genes allowing production of fully human IgG2kappa MAbs were used to rapidly create a panel of anti-HIV gp120 MAb-producing hybridomas by immunization with HIV SF162 gp120 -- several of the MAbs obtained were effective at neutralizing the autologous strain -- 8.22.2 was the only V2-specific MAb created and it could cross-compete with MAb 697D -- 8.22.2 could cross-react with BaL and JR-FL, two B clade R5 strains, but not B clade X4 or E clade viruses, and it could weakly neutralize autologous strain SF162. He2002 (antibody binding site, antibody generation, variant cross-reactivity, subtype comparisons)

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.

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.

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
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.

12b: This epitope is similar to a fragment of the human protein macrophage colony stimulating factor I receptor SISIRLKVQK. Maksiutov2002
12b: Neutralizes HXB2, but fails to neutralize chimeric virus with gp120 from primary isolates in an HXB2 background. McKeating1996b
12b: V2 MAb neutralized HXB2 -- position 179-180 LD to DL abrogates binding -- competes with 60b, but not 74. Shotton1995

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.

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
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.

B12 database note: This is a mouse MAb, distinct from the better-known human b12 bNAb.
B12: This antibody is not explicitly mentioned in Abacioglu1994, but this paper is referenced as the source of the antibody discussed by Moore1994a. Abacioglu1994 (antibody generation)
B12: This epitope is similar to a fragment of human protein lymphatic endothelium-specific hyaluronan receptor LYVE-1, TTRLLVQGSLRAEE. Maksiutov2002
B12: C2 region -- the relative affinity for denatured/native gp120 is 27 -- mutations 257 T/R and 262 N/T impair binding. Moore1994a

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.

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
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.

M89: This epitope is similar to a fragment of human protein lymphatic endothelium-specific hyaluronan receptor LYVE-1, TTRLLVQGSLRAEE. Maksiutov2002
M89: C2 region -- the relative affinity for denatured/native gp120 is >30 -- mutations 257 T/R and 269 E/L impair binding. Moore1994a
M89: Immunoblot reactive, RIP negative, for strains IIIB, 451, MN, RF, and RUTZ. Veronese1992

References

Showing 4 of 4 references.

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
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.

C13: NIH AIDS Research and Reference Reagent Program: 1209.
C13: This epitope is similar to a fragment of human protein lymphatic endothelium-specific hyaluronan receptor LYVE-1, TTRLLVQGSLRAEE. Maksiutov2002
C13: Epitope boundary extended to RPVVSTQLLLNGSLAEEEVVIR, to take into account the effect of a point mutation. Abacioglu1994
C13: The relative affinity for denatured/native gp120 is 36 -- mutations 257 T/R, 267 E/L, and 269 E/L impair binding. Moore1994a
C13: Bound preferentially to denatured IIIB gp120. Moore1993a

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.

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.

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
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.

110.E: This epitope is similar to a fragment of human protein lymphatic endothelium-specific hyaluronan receptor LYVE-1, TTRLLVQGSLRAEE. Maksiutov2002
110.E: The relative affinity for denatured/native gp120 is 7.3. Moore1994a

References

Showing 3 of 3 references.

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
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.

IIIB-V3-26: This epitope is similar to a fragment of the FasI receptor precursor (Apptosis-mediating surface antigen fas) (APO- 1 antigen) (CD95 antigen), VEINCTRQN. Maksiutov2002
IIIB-V3-26: Binds to the base of the V3 loop on denatured gp120. Laman1992

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.

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
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.

IIIB-V3-21: IIIB-V3-21 did not show any significant neutralization of infection of PBLs with various HIV-1 strains. IIIB-V3-21 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells, in contrast, it somewhat increased the passage of cell-free HIV-1 through the epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including IIIB-V3-21, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs. Chomont2008 (enhancing activity, neutralization)
EVA3048: EVA3048: Binding of HLA peptide HA307-319 to gp120 was not influenced by pre-incubation of gp120 with MAb EVA3048, indicating that this Ab does not completely occlude sequences/structures of the C5 gp120 region relevant for the C5 mimicry of the HLA activation domain. Cadogan2008 (mimics)
V3-21: Transmission of HIV-1 by immature and mature DCs to CD4+ T lymphocytes was significantly higher for CXCR4- than for CCR5-tropic strains. In addition, V3-21 inhibited transmission of CCR5-tropic viruses while transmission of V3-21-neutralized X4 variants increased, indicating that X4 HIV-1 has an advantage over R5 in transmission when neutralized with V3-21. vanMontfort2008 (co-receptor, neutralization, dendritic cells)
The role of DC-specific ICAM-grabbing nonintegrin (DC-SIGN) as a potential receptor for HIV-1 in the capture and transfer of neutralized HIV-1 to CD4 T lymphocytes was studied. The nonneutralizing V3-21 enhanced HIV-1 infection upon capture and transfer via Raji-DC-SIGN cells, whereas no infection was observed with the neutralizing b12 MAb, indicating that different Abs have variant effects on inhibiting HIV-1 transfer to CD4 T lymphocytes. vanMontfort2007 (enhancing activity, neutralization, dendritic cells)
IIIB-V3-21: The role of serine proteases on HIV infection was explored. Trypsin decreased the binding of most Env MAb tested and diminished cell fusion of H9 cells infected with HIV-1 LAI virus (H9/IIIB) to MAGI cells. In contrast, thrombin increased the binding of MAbs to gp120 epitopes near the CD4 and CCR5 binding sites, and increased cell fusion. Binding of the V3 MAbs 694-98D and 447-52D, that both bind near the tip of the loop, was decreased by both thrombin and trypsin, but anti-V3 MAb IIIB-V3-21 was not decreased in either case. Ling2004 (antibody binding site)
IIIB-V3-21: NIH AIDS Research and Reference Reagent Program: 1725.
IIIB-V3-21: UK Medical Research Council AIDS reagent: ARP3048.
IIIB-V3-21: This epitope is similar to a fragment of the FasI receptor precursor (Apptosis-mediating surface antigen fas) (APO- 1 antigen) (CD95 antigen), VEINCTRQN. Maksiutov2002
IIIB-V3-21: A rare mutation in the neutralization sensitive R2-strain in the proximal limb of the V3 region caused Env to become sensitive to neutralization by MAbs directed against the CD4 binding site (CD4BS), CD4-induced (CD4i) epitopes, soluble CD4 (sCD4), and HNS2, a broadly neutralizing sera -- 2/12 anti-V3 MAbs tested (19b and 694/98-D) neutralized R2, as did 2/3 anti-CD4BS MAbs (15e and IgG1b12), 2/2 CD4i MAbs (17b and 4.8D), and 2G12 and 2F5 -- thus multiple epitopes on R2 are functional targets for neutralization and the neutralization sensitivity profile of R2 is intermediate between the highly sensitive MN-TCLA strain and the typically resistant MN-primary strain. Zhang2002
IIIB-V3-21: Does not block HIV-1 LAI binding or entry into CEM cells. Valenzuela1998
IIIB-V3-21: Binds to NP40 treated gp120, and epitope is probably obscured by local glycosylation. Laman1993
IIIB-V3-21: Binds to the base of the V3 loop on denatured gp120. Laman1992

References

Showing 10 of 10 references.

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.

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
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.

M38: This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV, as well as to a fragment of IFN-related IFRD2 (PC4-B) protein, ARTKARSRVRDKRA. Maksiutov2002
M38: Infected individuals have HLA class I-gp120 cross-reactive antibodies. DeSantis1994
M38: Binds to the carboxy terminus of gp120, in a gp41 binding region, and also to denatured human HLAs (antigenic homology) Lopalco1993
M38: Binds to gp120 and to a 80 kd human protein expressed on a small fraction of mononuclear cells in the lymph nodes. Beretta1987

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.

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.

This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV, as well as to a fragment of IFN-related IFRD2 (PC4-B) protein, ARTKARSRVRDKRA. Maksiutov2002
Chimeric peptide combining two peptides gp160(495-516 and 584-612) served as a specific and broadly reactive antigen for diagnostic detection of HIV-1. Hernandez2000

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.

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
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.

110-1: Broadly reactive. Gosting1987 (antibody binding site, antibody generation)
110.1: Similarity level of the 110.1 binding site pentapeptide IPIHY to the host proteome was low, with the low-similarity 5-mer occurring in the host proteome 0 times, indicating that this peptide can be used to elicit Abs for active/passive immunotherapy with low risk of cross-reaction with the host proteome. Kanduc2008
110.1: Polyanionic polysaccharides were proposed to inhibit viral functions such as binding and syncytia formation through interactions mediated through the local high positive charge density in the V3 loop. The binding of this antibody is not inhibited by dextransulfate, in contrast to anti-V3 antibodies. Callahan1991
110.1: This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV. Maksiutov2002
110.1: Does not affect LAI viral binding or entry into CEM cells. Valenzuela1998
110.1: Does not neutralize HIV-1 LAI. McDougal1996
110.1: MAbs against the glycosphingolipid GalCer block HIV infection of normally susceptible CD4 negative cells from the brain and colon -- MAbs against the carboxy-terminus of gp120 inhibit gp120 binding to GalCer but not as potently as anti-V3 MAbs -- binding of GalCer to gp120 does not inhibit MAb binding. Cook1994
110.1: The relative affinity for denatured/native gp120 is 0.7. Moore1994a (antibody binding site)
110.1: Difference was noted in the epitope: mapped to aa 421-429 (KQIINMWQE), the T1 sequence -- poor efficacy as an immunotoxin when linked to RAC. Pincus1991 (antibody binding site, immunotoxin)
110.1: Referred to as 110-1 -- does not inhibit CD4-gp120 binding or neutralize HIV-1 strains. States that the Abs 110-1 and 110-4 were provided by M. Kathleen Shriver, Genetic Systems Corp. Linsley1988 (antibody binding site)
110.1: Database comment: There is another antibody with ID 110.1 that binds to gp120, but it is a human mAb that binds Env aa 200-217.

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.

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.

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.

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.

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.

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
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.

RV110026: This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV. Maksiutov2002
RV110026: Preferentially binds SDS-DTT denatured gp120 (15 fold using R1/87 as capture reagent) Moore1994a

References

Showing 3 of 3 references.

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
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.

43F: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 43F is discussed as the C5-targeting, non-neutralizing anti-gp120 mAb exhibiting ADCC activity and having a linear epitope. Pollara2013 (ADCC, review)
43F: This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV. Maksiutov2002
43F: 42F and 43F were isolated from a long term non-progressor by EBV transformation of PBMC -- samples were taken 14 months apart -- both MAbs stained diverse strains of infected cells and directed ADCC -- were more potent for ADCC if the cell was infected with HIV-1, rather than just presenting absorbed gp120. Alsmadi1997

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.

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
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.

42F: The complexity of the epitopes recognized by ADCC responses in HIV-1 infected individuals and candidate vaccine recipients is discussed in this review. 42F is discussed as the C5-targeting, non-neutralizing anti-gp120 mAb exhibiting ADCC activity and having a linear epitope. Pollara2013 (ADCC, review)
42F: This epitope is similar to a fragment of the human protein mast/stem cell growth factor receptor precursor, VVPTKADKRRSV. Maksiutov2002
42F: A study of 6 anti-Env MAbs and their ability to bind or direct ADCC against target cells infected with IIIB, MN, SF-2, and RF -- bound and directed lysis against strains IIIB, MN, SF-2, and RF, but not a clone of MN. Alsmadi1998 (ADCC)
42F: 42F and 43F were isolated from a long term non-progressor by EBV transformation of PBMC -- samples were taken 14 months apart -- both MAbs stained diverse strains of infected cells and directed ADCC -- were more potent for ADCC if the cell was infected with HIV-1, rather than just presenting absorbed gp120. Alsmadi1997 (ADCC)

References

Showing 4 of 4 references.

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.

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
Subtype	B
Ab Type
Neutralizing
Species (Isotype)	human(IgG1κ)
Patient
Immunogen	HIV-1 infection
Keywords

Notes

Showing 2 of 2 notes.

24G3: This epitope is similar to a fragment of the HLA class II histocompatibility antigen, GGSCMAALTVTLTV. Maksiutov2002
24G3: Human MAb generated by electrofusion of PBL from HIV-1+ volunteers with CB-F7 cells. Buchacher1992,Buchacher1994

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.

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
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.

1A1 database note: There are two distinct antibodies named 1A1.
1A1: This epitope is similar to a fragment of the HLA class II histocompatibility antigen, GGSCMAALTVTLTV. Maksiutov2002
1A1: Human MAb generated using EBV transformation of PBL from HIV-1+ volunteers. Buchacher1994 (antibody binding site, antibody generation)

References

Showing 2 of 2 references.

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
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.

25C2: This epitope is similar to a fragment of the HLA class II histocompatibility antigen, GGSCMAALTVTLTV. Maksiutov2002
25C2: Called IAM 41-25C2 -- Binding domain overlaps sites that are critical for gp120-gp41 association -- binding is enhanced by sCD4 -- binding region defined as: gp41(21-38 BH10). Sattentau1995 (antibody binding site)
25C2: Human MAb generated by electrofusion of PBL from HIV-1+ volunteers with CB-F7 cells -- binds oligomeric and monomeric gp41, and gp160. Buchacher1992,Buchacher1994 (antibody binding site, antibody generation)

References

Showing 4 of 4 references.

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.

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
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.

5F3: Interaction of 2F5 with its epitope and confirmation of core epitopes of 2F5 and 4E10 were reported. Epitope for non-neutralizing Ab 5F3 is identified as QNQQEKNE (650-657), located outside the MPER. Fiebig2009
Database note: Light chain has been updated to lambda (from kappa as reported in Buchacher et al). Information from Brittany Martin of AIDS Reagent Program and Dr. Dietmar Katinger of Polymun.
5F3: The capacity of 5F3 to block completely the activity of the anti-HIV peptide T20 was investigated. T20 inhibited the fusion or syncytia formation between co-cultured CHO-WT cells expressing HIV-1 HXB2 envelope glycoprotein on their surface and HeLaT4 cells. 5F3 was not able to block the anti-fusion effect of T20. Vincent2012 (antibody interactions)
5F3: The inhibitory activity of HIV-1-specific Abs against HIV-1 replication in langerhans cells (LCs) and interstitial dendritic cells (IDCs) was analyzed. Five well-known NAbs 447-52D, 4E10, b12, 2G12, 2F5 strongly inhibited HIV-1BaL and HIV-1TV1 replication in LCs and IDCs, and their inhibitory activities were stronger than those measured on PBMCs. Inhibition was more efficient by IgGs than corresponding IgAs, due to an Fc receptor-dependent mechanism, where HIV-1 inhibition occurs by binding of the Fc portion of IgGs to Fc receptors. Nonneutralizing noninhibitory Abs 5F3 and 3D6, directed against gp41, which did not exhibit any inhibitory activity in previous assays, also had no inhibitory effects in this model system. Peressin2011 (genital and mucosal immunity, dendritic cells)
5F3: To test whether HIV-1 particle maturation alters the conformation of the Env proteins, a sensitive and quantitative imaging-based Ab-binding assay was used to probe the conformations of full-length and cytoplasmic tail (CT) truncated Env proteins on mature and immature HIV-1 particles. MAb 5F3 binding to immature virions was approximately twice that of mature virions. When the CT was truncated, MAb 5F3 binding to mature particles was increased, but binding to mature and immature particles was equivalent. This suggested that virion maturation masked the epitope recognized by MAb 5F3, and truncation of the gp41 CT abolished this effect. Joyner2011 (binding affinity)
5F3: 58 mAbs, including 3 broadly neutralizing mAbs, were isolated from memory B cells of HIV-1 infected donors using an improved EBV immortalization method combined with a broad screening strategy. 5F3 competed for binding to gp41 with 6 of the new mAbs. Corti2010 (binding affinity)
5F3: 5F3 recognized trimeric and dimeric forms of cross-linked sgp140(-) Env JRFL glycoprotein. Yuan2009 (antibody binding site)
5F3: Although a substantial increase in neutralization potency of MPER-specific Abs 4E10 and 2F5 was observed in cells expressing FcγR I and IIb, no such effect was observed for 5F3. Perez2009 (neutralization)
5F3: 5F3 neutralized infection of PBLs with various HIV-1 strains. However, 5F3 did not inhibit transcytosis of cell-free or cell-associated virus across a monolayer of epithelial cells. A mixture of 13 MAbs directed to well-defined epitopes of the HIV-1 envelope, including 5F3, did not inhibit HIV-1 transcytosis, indicating that envelope epitopes involved in neutralization are not involved in mediating HIV-1 transcytosis. When the mixture of 13 MAbs and HIV-1 was incubated with polyclonal anti-human γ chain, the transcytosis was partially inhibited, indicating that agglutination of viral particles at the apical surface of cells may be critical for HIV transcytosis inhibition by HIV-specific Abs. Chomont2008 (neutralization)
5F3: 5F3 reacted with maltose-binding proteins MBP30 and MBP32, containing both HR1 and HR2 domains of gp41, but did not react with MBP37 and MBP44, containing only the HR2 domain, nor with MBP-HR1, containing only the HR1 domain. In addition, 5F3 bound to MBP44/N36 and MBP-HR1/C34 complexes reaching a plateau at a concentration of ˜ 1 µg/ml. In ELISA, 5F3 reacted with the complex formed between MBP-HR1 and H44 (His-targeted protein) and C34, but failed to recognize the mixture of MBP-HR1 and T20, MBP3 and C34, and MBP3 and H44. In addition, 5F3 recognized the peptide complex N36/C34 but not the peptides individually. Vincent2008 (antibody binding site)
5F3: Significant levels of 5F3 were shown to bind to HA/gp41 expressed on cell surfaces and this Ab did stain cells expressing HA/gp41 in a fluorescence assay. However, this Ab did not bind to the surfaces of HIV Env expressing cells and a much smaller percentage of the HIV 89.6 Env expressing cells were stained with this Ab than with 2G12, indicating that this Ab recognition site on gp41 is masked by the gp120 subunit in the HIV Env protein and that it is more easily accessible on the HA/gp41 chimeric protein. Ye2006 (antibody binding site, binding affinity)
5F3: This Ab was used in the analysis of clade C gp140 (97CN54) antigenicity and was shown to bind with relatively high avidity to the molecule and did not dissociate within 420 s. 5F3 was also used in a competition assay and shown to inhibit binding of N3C5 Ab by 80-90% and of N03B11 by 98-100%, indicating proximity of their epitopes. Sheppard2007a (antibody binding site, antibody interactions, kinetics, binding affinity)
5F3: Point mutations in the highly conserved structural motif LLP-2 within the intracytoplasmic tail of gp41 resulted in conformational alternations of both gp41 and gp120. The alternations did not affect virus CD4 binding, coreceptor binding site exposure, or infectivity of the virus, but did result in decreased binding of certain MAbs and increased neutralization resistance to MAbs as well as to human polyclonal HIV-Ig and pooled human sera. 5F3 MAb did not neutralize the LLP-2 mutant nor the wildtype virus. 5F3 exhibited similar levels of binding to both LLP-2 mutant and the wildtype virus. Kalia2005 (antibody binding site, neutralization, binding affinity)
5F3: This Ab did not inhibit HIV-1 BaL replication in macrophages. Holl2006 (neutralization, dendritic cells)
5F3: This epitope is similar to a fragment of the HLA class II histocompatibility antigen, GGSCMAALTVTLTV. Maksiutov2002
5F3: Human MAb generated by electrofusion of PBL from HIV-1+ volunteers with CB-F7 cells. Epitope was found at 526-543 (AAGSTMGAASMTLTVQARQ?) of HIV-1 isolate BH10. IgG subtype was reported as IgG₁ with κ light chain. Later, in Fiebig2009, it was shown that the light chain is λ and the epitope is actually QNQQEKNE (650-657). Buchacher1994 (antibody binding site, antibody generation)

References

Showing 15 of 15 references.

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.

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.

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
Ab Type
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine component	Nef

Notes

Showing 2 of 2 notes.

AM5C6: This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
AM5C6: Epitope mapped by overlapping decapeptides -- core: SRDL -- also reacts with Nef(78-92). Schneider1991

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.

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
Ab Type
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine component	Nef

Notes

Showing 2 of 2 notes.

26/76: This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
26/76: Epitope mapped by overlapping decapeptides -- core: SRDLEK. Schneider1991

References

Showing 2 of 2 references.

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
Ab Type
Neutralizing
Species (Isotype)	mouse
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine component	Nef

Notes

Showing 2 of 2 notes.

25/03: This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
25/03: Epitope mapped by overlapping decapeptides -- core: ASRDLEK. Schneider1991

References

Showing 2 of 2 references.

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
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.

3F2: UK Medical Research Council AIDS reagent: EVA3067.1.
3F2: This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
3F2: Faintly cross-reactive with astrocytes of uninfected control samples. Ranki1995
3F2: Reacted with Nef from different HIV-1 strains (BRU, IIIB, RF, MN). Ovod1992

References

Showing 4 of 4 references.

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 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
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.

3D12: UK Medical Research Council AIDS reagent: EVA3067.2.
3D12: This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
3D12: One of four antibodies used in combination to show HIV Nef protein expressed in astrocytes from 7/14 brain samples from HIV+ individuals -- Nef expression associated with dementia. Ranki1995
3D12: Over-expression of Nef in astrocytes from postmortem pediatric CNS tissues. Saito1994
3D12: Reacted with Nef from different HIV-1 strains (BRU, IIIB, RF, MN). Ovod1992
3D12: Database comment: There is an anti-RT MAb that is also named 3D12.

References

Showing 4 of 4 references.

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.

This epitope is similar to a fragment of the human protein vascular endothelial growth factor C, AEPDAGEATAYASKDLE. Maksiutov2002
Nef encapsulated in poly(DL-lactide-co-glycolide) (PLG) had a more prolonged Ab response than Nef in PBS or in Freund's adjuvant (CFA), still strong after 7 months -- the response was predominantly IgG1, a Th2 immune response -- three linear epitopes, Nef 32-64, 118-167, and 185-205, were frequently recognized by the sera of mice immunized with NefPLG or Nef-CFA, but not after immunization with Nef in PBS, which seemed to preferentially stimulate an Ab response to conformational epitopes. Moureau2002

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.

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.

This epitope is similar to a fragment of the human protein Bone-derived growth factor, PLEPAKLEE, and to Hematopoietic progenitor cell antigen CD34, TSLHPVSQHG. Maksiutov2002
Nef encapsulated in poly(DL-lactide-co-glycolide) (PLG) had a more prolonged Ab response than Nef in PBS or in Freund's adjuvant (CFA), still strong after 7 months -- the response was predominantly IgG1, a Th2 immune response -- three linear epitopes, Nef 32-64, 118-167, and 185-205, were frequently recognized by the sera of mice immunized with NefPLG or Nef-CFA, but not after immunization with Nef in PBS, which seemed to preferentially stimulate an Ab response to conformational epitopes. Moureau2002

References

Showing 2 of 2 references.

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
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.

2F2 database note: There are two distinct antibodies named 2F2 in the database.
2F2: UK Medical Research Council AIDS reagent: EVA3067.3.
2F2: This epitope is similar to a fragment of the human protein Hematopoietic progenitor cell antigen CD34, TSLHPVSQHG. Maksiutov2002
2F2: One of four antibodies used in combination to show HIV Nef protein expressed in astrocytes from 7/14 brain samples from HIV+ individuals -- Nef expression associated with dementia. Ranki1995
2F2: Over-expression of Nef in astrocytes from postmortem pediatric CNS tissue. Saito1994
2F2: Strain specific (MN and BRU reactive, not IIIB or RF). Ovod1992

References

Showing 4 of 4 references.

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.

E9: This epitope is similar to a fragment of the human protein Hematopoietic progenitor cell antigen CD34, TSLHPVSQHG. Maksiutov2002
E9: Insect cells expressing myristylated Nef proteins on their cell surface can induce cytolysis of unstimulated CD4+ cells -- this response is not due to MHC restricted CTL activity -- the cell surface of Nef expressing insect cells carry Nef that can be recognized by MAbs E7 and E9 but not F1. Fujii1996
E9: A carboxy-terminal domain of Nef on the cell surface induces cytolysis of CD4+ T cells. Fujii1996b
E9: The C-term end of Nef is accessible to Abs at the cell surface -- stained IIIB/M10, but not MN/M10, cells. Fujii1993,Otake1994

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.

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
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.

3E6: UK Medical Research Council AIDS reagent: EVA3067.4.
3E6: This epitope is similar to a fragment of the human protein Hematopoietic progenitor cell antigen CD34, TSLHPVSQHG. Maksiutov2002
3E6: Faintly cross-reactive with astrocytes of uninfected control samples. Ranki1995
3E6: Reacted with Nef from different HIV-1 strains (BRU, IIIB, RF, MN). Ovod1992

References

Showing 4 of 4 references.