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Displaying record number 309

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MAb ID	W1
HXB2 Location	gp160(102-121) DNA(6528..6587)	gp160 Epitope Map
Author Location	gp120(102-121 LAI)
Research Contact	D. Weiner, U. Penn.
Epitope	EQMHEDIISLWDQSLKPCVK	Epitope Alignment
Subtype	B
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	mouse(IgG)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 1 of 1 note.

• W1: The relative affinity for denatured/native gp120 is 6 -- mutations 113 D/A, 113 D/R, and 117 K/W impair binding. Moore1994a

References

Showing 1 of 1 reference.

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 292

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MAb ID	11/65 (11/65a/5h)
HXB2 Location	gp160(102-121) DNA(6528..6587)	gp160 Epitope Map
Author Location	gp120(311-321 HXB10)
Epitope	EQMHEDIISLWDQSLKPCVK	Epitope Alignment
Ab Type	gp120 C1
Neutralizing
Species (Isotype)	rat(IgG2b)
Patient
Immunogen	vaccine
Keywords

Vaccine Details

Notes

Showing 3 of 3 notes.

• 11/65: UK Medical Research Council AIDS reagent: ARP3076.
• 11/65: Called 11/65a/5h -- The most variable amino acids in the V3 loop were replaced with serines to make the immunodominant V3 loop less immunogenic -- these changes did not affect the ability of sCD4 or MAbs to V1/V2, C1 and C4 to bind -- 11/65 was not affected by V3 serine substitutions -- mice injected with serine substituted gp120 had a reduced response relative to wildtype, and no enhanced immunogenicity of conserved regions. Peet1998
• 11/65: Binds only soluble gp120, not virion bound -- used to quantify gp120 shedding -- (numbering is incorrect in original?) McKeating1992a

References

Showing 3 of 3 references.

McKeating1992a J. A. McKeating, J. Cordell, C. J. Dean, and P. Balfe. Synergistic Interaction between Ligands Binding to the CD4 Binding Site and V3 Domain of Human Immunodeficiency Virus Type I gp120. Virology, 191:732-742, 1992. PubMed ID: 1280382. Show all entries for this paper.

McKeating1993a J. A. McKeating, C. Shotton, J. Cordell, S. Graham, P. Balfe, N. Sullivan, M. Charles, M. Page, A. Bolmstedt, S. Olofsson, S. C. Kayman, Z. Wu, A. Pinter, C. Dean, J. Sodroski, and R. A. Weiss. Characterization of neutralizing monoclonal antibodies to linear and conformation-dependent epitopes within the first and second variable domains of human immunodeficiency virus type 1 gp120. J. Virol., 67:4932-4944, 1993. Substitutions in the V2 loop can result in complete dissociation of gp120 and gp41, suggesting alterations in V2 can affect subunit assembly. Other substitutions allowed gp120-gp41 association and expression, but inhibited viral entry or syncytia. Binding of some neutralizing MAbs was altered by V2 substitutions. For MAb CRA-4, changes at residues 191/192/193 (YSL/GSS), and for 11/68b, changes at residues 183/184 (PI/SG), within V2, and for both MAbs a position 435 (Y/H) change in C4, abrogate binding. These MAbs can bind to V1 and V2 domains in the absence of C4 domain, so the C4 substitution probably results in conformational change. PubMed ID: 7687306. Show all entries for this paper.

Peet1998 N. M. Peet, J. A. McKeating, J. B. de Souza, I. M. Roitt, P. J. Delves, and T. Lund. The Effect of Low-Profile Serine Substitutions in the V3 Loop of HIV-1. Virology, 251:59-70, 1998. PubMed ID: 9813203. Show all entries for this paper.