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Vaccine Details

Notes

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• 11/68b: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
• 11/68b: UK Medical Research Council AIDS reagent: ARP3041.
• 11/68b: 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 -- 11/68b 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
• 11/68b: Cross-competes with MAbs 62c, 66c, 66a, and CRA-4 -- similar to MAb 62c -- HXB2 neutralization escape mutant had a D/N substitution at residue 185 -- non-reciprocal inhibition of binding of CRA-3 and CRA-6. Shotton1995
• 11/68b: 435 (Y/H) in C4 does not abrogate binding (John Moore, per comm, 1996).
• 11/68b: Changes at residues 183/184 (PI/SG) within V2, 435 (Y/H) in C4, abrogate binding. McKeating1993a

References

Showing 4 of 4 references.

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.

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.

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.

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.