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Displaying record number 3215

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MAb ID	2297
HXB2 Location	gp160	gp160 Epitope Map
Author Location
Epitope
Subtype	B
Ab Type	gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing
Species (Isotype)	human
Patient
Immunogen	HIV-1 infection
Keywords	binding affinity, glycosylation, neutralization, vaccine antigen design, vaccine-induced immune responses

Notes

Showing 3 of 3 notes.

2297: 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)
2297: The study compared various factors affecting the accessibility of epitopes for antibodies targeting the V2 integrin (V2i) region, versus the V3 region. CD4 treament of BaL and JRFL pseudoviruses increased their neutralization sensitivity to V3 MAbs, but not to V2i MAbs. Viruses grown in a glycosidase inhibitor were more sensitive to neutralization by V3, but not V2i, MAbs. Increasing the time of virus-MAb interaction increased virus neutralization by some V2i MAbs and all V3 MAbs. The structural dynamics of V2i and V3 epitopes has important effects in neutralization. The V2i MAbs tested were: 697, 830A, 1357, 1361, 1393, 2158, and 2297. Upadhyay2014 (glycosylation, neutralization)
2297: This study characterized the Elisa cross-reactivity, neutralization, and Ig variable genes of a panel of 7 anti-V2 mAbs: 1361, 1393A, 1357, 697, 830A, 2158, and 2297. Despite sequence variability, the 7 mAbs recognize conserved immunologic features of V2, with 6 of them targeting similar epitopes. The crystal structure of the mAb 697 binding site was determined. Gorny2012 (neutralization)

References

Showing 3 of 3 references.

Isolation Paper
Gorny2012 Miroslaw K. Gorny, Ruimin Pan, Constance Williams, Xiao-Hong Wang, Barbara Volsky, Timothy O'Neal, Brett Spurrier, Jared M. Sampson, Liuzhe Li, Michael S. Seaman, Xiang-Peng Kong, and Susan Zolla-Pazner. Functional and Immunochemical Cross-Reactivity of V2-Specific Monoclonal Antibodies from HIV-1-Infected Individuals. Virology, 427(2):198-207, 5 Jun 2012. PubMed ID: 22402248. Show all entries for this paper.

Upadhyay2014 Chitra Upadhyay, Luzia M. Mayr, Jing Zhang, Rajnish Kumar, Miroslaw K. Gorny, Arthur Nádas, Susan Zolla-Pazner, and Catarina E. Hioe. Distinct Mechanisms Regulate Exposure of Neutralizing Epitopes in the V2 and V3 Loops of HIV-1 Envelope. J. Virol., 88(21):12853-12865, Nov 2014. PubMed ID: 25165106. 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.