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Displaying record number 270

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MAb ID	133/192
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Research Contact	Matthias Niedrig
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing	L
Species (Isotype)	mouse(IgG1)
Patient
Immunogen	vaccine
Keywords	vaccine antigen design

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade IIIB
Vaccine component	gp120

Notes

Showing 8 of 8 notes.

• 133/192: 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 133/192. Pantophlet2004 (vaccine antigen design)
• 133/192: A gp120 molecule was designed to focus the immune response onto the IgG1b12 epitope. Ala substitutions that enhance the binding of IgG1b12 and reduce the binding of non-neutralizing MAbs were combined with additional N-linked glycosylation site sequons inhibiting binding of non-neutralizing MAbs; b12 bound to the mutated gp120. C1 and C5 were also removed, but this compromised b12 binding. Pantophlet2003b (vaccine antigen design)
• 133/192: 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
• 133/192: Does not neutralize JR-FL nor block gp120 interaction with CCR-5 in a MIP-1beta-CCR-5 competition study. Trkola1996b
• 133/192: Reciprocal binding inhibition with the antibody 4A7C6 -- enhanced by some anti-C5 and-C1 antibodies. Moore1996
• 133/192: C1 region -- substitutions 76P/Y, 113 D/A or R, 117 K/W, 420 I/R, 427 W/S impair binding, other substitutions enhanced binding. Moore1994c
• 133/192: The relative affinity for denatured/native gp120 is 1.8. Moore1994a
• 133/192: Epitope seems complex, binds multiple peptides -- weak neutralization of lab strain. Niedrig1992

References

Showing 10 of 10 references.

Niedrig1992 M. Niedrig, H.-P. Harthus, M. Broker, H. Bickhard, G. Pauli, H. R. Gelderblom, and B. Wahren. Inhibition of viral replication by monoclonal antibodies directed against human immunodeficiency virus gp120. J. Gen. Virol., 73:2451-2455, 1992. PubMed ID: 1383412. Show all entries for this paper.

Moore1993c J. P. Moore, M. Thali, B. A. Jameson, F. Vignaux, G. K. Lewis, S.-W. Poon, M. S. Fung, P. J. Durda, L. Akerblom, B. Wahren, D. D. Ho, Q. J. Sattentau, and J. Sodroski. Immunochemical Analysis of the gp120 Surface Glycoprotein of Human Immunodeficiency Virus Type 1: Probing the Structure of the C4 and V4 Domains and the Interaction of the C4 Domain with the V3 Loop. J. Virol., 73:4785-4796, 1993. General observations: C4 and V3 MAbs are sensitive to the way the epitopes are presented, and this sensitivity cannot be correlated to peptide binding. Some V3-C4 domain interaction was indicated based on mutation and interference studies. PubMed ID: 7687303. Show all entries for this paper.

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

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

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.

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.

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.

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.

Pantophlet2003b Ralph Pantophlet, Ian A. Wilson, and Dennis R. Burton. Hyperglycosylated Mutants of Human Immunodeficiency Virus (HIV) Type 1 Monomeric gp120 as Novel Antigens for HIV Vaccine Design. J. Virol., 77(10):5889-8901, May 2003. PubMed ID: 12719582. 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.

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Displaying record number 271

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MAb ID	C6 (Ch6)
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
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.

• C6: NIH AIDS Research and Reference Reagent Program: 810.
• C6: Called Ch6 -- binds to gp120 but not to infected cells -- when linked to ricin A, the immunotoxin did not mediate cell killing -- sCD4 has no effect. Pincus1993,Pincus1996
• C6: There is FNM/FDM polymorphism in LAI-based peptides -- N is essential (J. P. Moore, per. comm.)
• C6: The relative affinity for denatured/native gp120 is 0.9. Moore1994a
• C6: C1 region -- epitope boundaries mapped by peptide scanning, FNMW core. Abacioglu1994

References

Showing 4 of 4 references.

Pincus1993 S. H. Pincus and J. McClure. Soluble CD4 Enhances the Efficacy of Immunotoxins Directed against gp41 of the Human Immunodeficiency Virus. Proc. Natl. Acad. Sci. U.S.A., 90:332-336, 1993. PubMed ID: 8419938. 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.

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.

Pincus1996 S. H. Pincus, K. Wehrly, R. Cole, H. Fang, G. K. Lewis, J. McClure, A. J. Conley, B. Wahren, M. R. Posner, A. L. Notkins, S. A. Tilley, A. Pinter, L. Eiden, M. Teintze, D. Dorward, and V. V. Tolstikov. In Vitro Effects of Anti-HIV Immunotoxins Directed against Multiple Epitopes on HIV Type 1 Envelope Glycoprotein 160. AIDS Res. Hum. Retroviruses, 12:1041-1051, 1996. A panel of anti-gp160 MAbs to was used to construct anti-HIV immunotoxins by coupling antibodies to ricin A chain (RAC). The ability of the immunotoxins to kill HIV-1-infected cells was tested in tissue culture. Immunotoxins that bind epitopes on the cell surface killed infected cells, although killing was not directly proportional to binding. The activity of anti-gp41 immunotoxins was markedly enhanced in the presence of sCD4. PubMed ID: 8827220. Show all entries for this paper.

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Displaying record number 272

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MAb ID	B2
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG2b)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade LAI
Vaccine component	gp160

Notes

Showing 3 of 3 notes.

• B2: There is FNM/FDM polymorphism in LAI-based peptides, and N is essential (J. P. Moore, per. comm.)
• B2: The relative affinity for denatured/native gp120 is 1.4. Moore1994a
• B2: C1 region -- epitope boundaries mapped by peptide scanning, FNMW core. Abacioglu1994

References

Showing 5 of 5 references.

Thali1993 M. Thali, J. P. Moore, C. Furman, M. Charles, D. D. Ho, J. Robinson, and J. Sodroski. Characterization of Conserved Human Immunodeficiency Virus Type 1 gp120 Neutralization Epitopes Exposed upon gp120-CD4 Binding. J. Virol., 67:3978-3988, 1993. Five regions are likely to contribute to the 48d and 17b discontinuous epitopes, either directly or through local conformational effects: the hydrophobic ring-like structure formed by the disulfide bond that links C3 and C4, the base of the stem-loop that contains V1 and V2, and the hydrophobic region in C2 from Arg 252 to Asp 262. Additionally changes in Glu 370, and Met 475 in C5, affected binding and neutralization. The hydrophobic character of these critical regions is consistent with the limited exposure on gp120 prior to CD4 binding. PubMed ID: 7685405. 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.

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

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

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.

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Displaying record number 278

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MAb ID	B10
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG1)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade LAI
Vaccine component	gp160

Notes

Showing 3 of 3 notes.

• B10: There is FNM/FDM polymorphism in LAI-based peptides, and N is essential (J. P. Moore, per. comm.)
• B10: The relative affinity for denatured/native gp120 is 0.4. Moore1994a
• B10: C1 region -- epitope boundaries mapped by peptide scanning, FNMW core. Abacioglu1994

References

Showing 3 of 3 references.

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.

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.

Yang2018 Zheng Yang, Xi Liu, Zehua Sun, Jingjing Li, Weiguo Tan, Weiye Yu, and Meiyun Zhang. Identification of a HIV gp41-Specific Human Monoclonal Antibody with Potent Antibody-Dependent Cellular Cytotoxicity. Front. Immunol., 9:2613, 2018. PubMed ID: 30519238. Show all entries for this paper.

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Displaying record number 282

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MAb ID	489.1(961)
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Research Contact	C. Bruck, SKB, Belgium
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine strain	B clade LAI
Vaccine component	Env

Notes

Showing 2 of 2 notes.

• 489.1(961): NIH AIDS Research and Reference Reagent Program: 961.
• 489.1(961): The relative affinity for denatured/native gp120 is 1. Moore1994a

References

Showing 1 of 1 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.

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Displaying record number 283

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MAb ID	T1.1
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	vaccinia
Vaccine component	gp160

Notes

Showing 3 of 3 notes.

• T1.1: C1 region -- the relative affinity for denatured/native gp120 is 1. Moore1994a
• T1.1: No ADCC activity -- reactive peptide: NVTENFNMWKNDMVEQ, IIIB. Broliden1990
• T1.1: Also reacted in solid phase with gp120(234-248) NGTGPCTNVSTQCT. Akerblom1990

References

Showing 3 of 3 references.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Broliden1990 P. A. Broliden, K. Ljunggren, J. Hinkula, E. Norrby, L. Akerblom, and B. Wahren. A monoclonal antibody to human immunodeficiency virus type 1 which mediates cellular cytotoxicity and neutralization. J. Virol., 64:936-940, 1990. PubMed ID: 2296090. Show all entries for this paper.

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

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Displaying record number 284

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MAb ID	T7.1
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine strain	B clade LAI
Vaccine component	Env

Notes

Showing 1 of 1 note.

• T7.1: The relative affinity of denatured/native gp120 is 4.0. Moore1994a

References

Showing 4 of 4 reference.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

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

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

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Displaying record number 285

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MAb ID	T9
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(gp120 91-100 LAI)
Research Contact	Lennart Akerblom, Britta Wahren and Jorma Hinkula
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine strain	B clade LAI
Vaccine component	Env

Notes

Showing 3 of 3 notes.

• T9: Binds to the C1 region -- 45 W/S, 88 N/P, 256 S/Y, 262 N/T, 475 M/S, 485 1.83, and 491 I/F enhanced binding, no substitution tested significantly inhibited. Moore1994c
• T9: The relative affinity of denatured/native gp120 is 7.9. Moore1994a
• T9 database comment: There are two HIV-Abs with the name T9, one binds to gp41, one to gp120.

References

Showing 5 of 5 references.

Akerblom1990 L. Akerblom, J. Hinkula, P.-A. Broliden, B. Makitalo, T. Fridberger, J. Rosen, M. Villacres-Eriksson, B. Morein, and B. Wahren. Neutralizing cross-reactive and non-neutralizing monoclonal antibodies to HIV-1 gp120. AIDS, 4:953-960, 1990. PubMed ID: 1702001. Show all entries for this paper.

Bolmstedt1992 A. Bolmstedt, S. Olofsson, E. Sjogren-Jansson, I. Sjoblom, L. Akerblom, J.-E. S. Hansen, and S.-L. Hu. Carbohydrate Determinant NeuAc-Gal-beta(1-4) of N-Linked Glycans Modulates the Antigenic Activity of Human Immunodeficiency Virus Type 1 Glycoprotein gp120. J. Gen. Virol., 73:3009-3105, 1990. PubMed ID: 1281869. Show all entries for this paper.

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

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

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.

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Displaying record number 286

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MAb ID	5B3
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine type	protein
Vaccine strain	B clade IIIB
Vaccine component	gp160

Notes

Showing 3 of 3 notes.

• 5B3: The relative affinity of denatured/native gp120 is 8.3. Moore1994a
• 5B3: Cross-blocks 1D10 in competitive IIIB-rsgp160 ELISA -- no neutralization -- blocks IIIB-gp120 sCD4 binding -- localized binding to residues 72-106. Nakamura1992
• 5B3: Blocks gp120 -CD4 binding. Berman1991

References

Showing 4 of 4 references.

Berman1991 P. W. Berman, K. Rosenthal, G. Nakamura, L. Riddle, J. P. Porter, D. Dowbenko, M. Hobbes, R. Byrn, J. Groopman, T. Gregory, and B. Fendly. Monoclonal Antibodies to gp160 of HIV-1 That Neutralize HIV-1 Infectivity, Block the Binding of gp120 to CD4, and React with Diverse Isolates. J. Acquir. Immune Defic. Syndr., 4:306, 1991. Show all entries for this paper.

Nakamura1992 G. R. Nakamura, R. Byrn, K. Rosenthal, J. P. Porter, M. R. Hobbs, L. Riddle, D. J. Eastman, D. Dowbenko, T. Gregory, B. M. Fendly, and P. W. Berman. Monoclonal Antibodies to the Extracellular Domain of HIV-1 IIIB gp160 That Neutralize Infectivity, Block Binding to CD4 React with Diverse Isolates. AIDS Res. Hum. Retroviruses, 8:1875-1885, 1992. PubMed ID: 1283308. 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.

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.

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Displaying record number 287

Download this epitope record as JSON.

MAb ID	MF49.1
HXB2 Location	gp160(91-100) DNA(6495..6524)	gp160 Epitope Map
Author Location	gp120(91-100 LAI)
Epitope	ENFDMWKNDM	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Vaccine strain	B clade LAI
Vaccine component	Env

Notes

Showing 1 of 1 note.

• MF49.1: The relative affinity of denatured/native gp120 is 3.8. Moore1994a

References

Showing 2 of 2 reference.

Thiriart1989 C. Thiriart, M. Francotte, J. Cohen, C. Collignon, A. Delers, S. Kummert, C. Molitor, D. Gilles, P. Roelants, F. Van Wijnendaele, M. De Wilde, and C. Bruck. Several Antigenic Determinants Exposed on the gp120 Moiety of HIV-1 gp160 Are Hidden on the Mature gp120. J. Immunol., 143:1832-1836, 1989. PubMed ID: 2476484. Show all entries for this paper.

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

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