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MAb ID	858-D (858-30D)
HXB2 Location	gp160(505-511) DNA(7737..7757)	gp160 Epitope Map
Author Location	gp120(510-516 LAI)
Research Contact	Susan Zolla-Pazner (Zollas01@mcrcr6.med.nyu) (NYU Med. Center)
Epitope	VVQREKR	Epitope Alignment
Subtype	B
Ab Type	C-term
Neutralizing
Species (Isotype)	human(IgG)
Patient
Immunogen	HIV-1 infection
Keywords	antibody binding site, antibody generation, binding affinity, dendritic cells, neutralization, vaccine antigen design, vaccine-induced immune responses

Notes

Showing 6 of 6 notes.

• 858-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)
• 858-D: This Ab did not inhibit HIV-1 BaL replication in macrophages or in PHA-stimulated PBMCs. Holl2006 (neutralization, dendritic cells)
• 858-D: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 4 C5 MAbs, 2 bound well, 2 bound weakly -- MAb 858-D bound only 4/26, the worst of all anti-C5 MAbs tested, while MAb 1331A, which shares the same core epitope (positions 495-516), bound to 18/26 isolates. Nyambi2000
• 858-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 -- C5 MAbs 858-D, 989-D and 1331A bound with a 5-10 fold preference for the monomer. Gorny2000b
• 858-D: No neutralizing activity, no ADCC activity, and no viral enhancing activity. Epitope numbering provided (gp120 510-516) does not correspond to the previously published (Zolla-Pazner1995) epitope VVQREKR. Forthal1995
• 858-D: Group specific cross-clade binding in serotyping study using flow-cytometry. Antibody produced by heterohybridomas derived from the PBMCs of HIV-infected individuals. Epitope is shown as VVQREKR, but determination of the epitope is not shown. Zolla-Pazner1995 (antibody binding site, antibody generation)

References

Showing 6 of 6 references.

Isolation Paper
Zolla-Pazner1995 S. Zolla-Pazner, J. O'Leary, S. Burda, M. K. Gorny, M. Kim, J. Mascola, and F. McCutchan. Serotyping of primary human immunodeficiency virus type 1 isolates from diverse geographic locations by flow cytometry. J. Virol., 69:3807-3815, 1995. A set of 13 human MAbs to a variety of epitopes were tested against a panel of primary isolates of HIV-1, representing different genetic clades. The V3 loop tended to be B clade restricted, and a single gp120 C-terminus binding antibody was clade specific. Two other gp120 C-terminus binding antibodies were group specific. PubMed ID: 7745728. 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.

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.

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.

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.

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.