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Displaying record number 525

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Notes

Showing 8 of 8 notes.

• C12: This study uncovered a potentially significant contribution of V_H replacement products which are highly enriched in IgH genes for the generation of anti-HIV Abs including anti-gp41, anti-V3 loop, anti-gp120, CD4i and PGT Abs. The V_H replacement "footprints" within CD4i Abs preferentially encode negatively charged amino acids within IgH CDR3. The details of C12 V_H replacement products in IgH gene and mutations and amino acid sequence analysis are described in Table 1,Table 2 and Fig 3. Liao2013a (antibody sequence)
• C12: The Ig usage for variable heavy chain of this Ab was as follows: IGHV:1-69, IGHD:nd, D-RF:nd, IGHJ:4. Non-V3 mAbs preferentially used the VH1-69 gene segment. In contrast to V3 mAbs, these non-V3 mAbs used several VH4 gene segments and the D3-9 gene segment. Similarly to the V3 mAbs, the non-V3 mAbs used the VH3 gene family in a reduced manner. Anti-CD4i mAbs exclusively used the VH1 gene family. Gorny2009 (antibody sequence)
• C12: Tyrosine sulfation of C12 and other Abs, and its effect on Ab binding and neutralization, is reviewed. Lin2007 (review)
• C12: C12 was obtained from an HIV-1 infected individual with a potent and broadly neutralizing activity of his serum. It was shown that scFv C12 was sulfate-modified and it is implied that the sulfates are localized exclusively within the heavy chain CDR3 region of this MAb. Binding efficiency of scFv C12 to ADA gp120 was doubled in the presence of CD4, showing that this MAb is a CD4-induced. Association of scFv C12 with ADA gp120-CD4-Ig complex was partially inhibited by a sulfated peptide with a sequence corresponding to the CCR5 amino terminus, indicating that C12 binds a CD4-enhanced epitope overlapping the binding domain of CCR5 amino terminus. scFv C12 was shown to efficiently bind to gp120 of three R5 isolates but not to the HXBc2 X4 isolate. Choe2003 (antibody binding site, co-receptor)
• C12: The CDR3 regions of CD4i Abs (E51, 412d, 17b, C12 and 47e) were cloned onto human IgG1 and tested for their ability to inhibit CCR5 binding. Only E51 successfully immunoprecipitated gp120. Dorfman2006 (co-receptor)
• C12: C3 region -- epitope boundaries mapped by peptide scanning, core FNCGG. Abacioglu1994
• C12: The relative affinity for denatured/native gp120 is >30 -- mutations 380 G/F, 381 E/P, and 384 Y/E impair binding -- also binds GEFFYCNSTQLFNS, gp120(380-393 LAI) Moore1994a
• C12: Bound preferentially to denatured IIIB gp120. Moore1993a

References

Showing 9 of 9 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.

Choe2003 Hyeryun Choe, Wenhui Li, Paulette L. Wright, Natalya Vasilieva, Miro Venturi, Chih-Chin Huang, Christoph Grundner, Tatyana Dorfman, Michael B. Zwick, Liping Wang, Eric S. Rosenberg, Peter D. Kwong, Dennis R. Burton, James E. Robinson, Joseph G. Sodroski, and Michael Farzan. Tyrosine Sulfation of Human Antibodies Contributes to Recognition of the CCR5 Binding Region of HIV-1 gp120. Cell, 114(2):161-170, 25 Jul 2003. PubMed ID: 12887918. Show all entries for this paper.

Dorfman2006 Tatyana Dorfman, Michael J. Moore, Alexander C. Guth, Hyeryun Choe, and Michael Farzan. A Tyrosine-Sulfated Peptide Derived from the Heavy-Chain CDR3 Region of an HIV-1-Neutralizing Antibody Binds gp120 and Inhibits HIV-1 Infection. J. Biol. Chem., 281(39):28529-28535, 29 Sep 2006. PubMed ID: 16849323. Show all entries for this paper.

Lin2007 George Lin and Peter L. Nara. Designing Immunogens to Elicit Broadly Neutralizing Antibodies to the HIV-1 Envelope Glycoprotein. Curr. HIV Res., 5(6):514-541, Nov 2007. PubMed ID: 18045109. Show all entries for this paper.

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

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

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.

Gorny2009 Miroslaw K. Gorny, Xiao-Hong Wang, Constance Williams, Barbara Volsky, Kathy Revesz, Bradley Witover, Sherri Burda, Mateusz Urbanski, Phillipe Nyambi, Chavdar Krachmarov, Abraham Pinter, Susan Zolla-Pazner, and Arthur Nadas. Preferential Use of the VH5-51 Gene Segment by the Human Immune Response to Code for Antibodies against the V3 Domain of HIV-1. Mol. Immunol., 46(5):917-926, Feb 2009. PubMed ID: 18952295. Show all entries for this paper.

Liao2013a Hongyan Liao, Jun-tao Guo, Miles D. Lange, Run Fan, Michael Zemlin, Kaihong Su, Yongjun Guan, and Zhixin Zhang. Contribution of V(H) Replacement Products to the Generation of Anti-HIV Antibodies. Clin. Immunol., 146(1):46-55, Jan 2013. PubMed ID: 23220404. Show all entries for this paper.

Displaying record number 524

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Vaccine Details

Notes

Showing 2 of 2 notes.

• 36.1: UK Medical Research Council AIDS reagent: ARP329.
• 36.1: The relative affinity for denatured/native gp120 is >30 -- mutations 380 G/F, 381 E/P impair binding. Moore1994a

References

Showing 2 of 2 references.

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.