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Displaying record number 953

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MAb ID	1393A
HXB2 Location	Env	Env Epitope Map
Author Location	gp120
Epitope
Subtype	B
Ab Type	gp120 V2 // V2 glycan(V2g) // V2 apex
Neutralizing	P (tier 1) View neutralization details
Species (Isotype)	human
Patient	donor_uncoded_1
Immunogen	HIV-1 infection
Keywords	binding affinity, glycosylation, neutralization, review, subtype comparisons, vaccine antigen design, vaccine-induced immune responses

Notes

Showing 5 of 5 notes.

1393A: 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)
1393A: 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)
1393A: 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)
1393A: This broad review of anti-Envelope MAbs notes that V2 MAbs are generally weakly neutralizing at best, and somewhat strain specific. Anti-V2 MAbs 1357, 1361, 1393A are non-neutralizing. Gorny2003 (review)
1393A: 26 HIV-1 group M isolates (clades A to H) were tested for binding to 47 MAbs, including 5 anti-V2 MAbs, which showed weak and sporadic binding, with the most frequent binding to C and D clades. Nyambi2000 (subtype comparisons)

References

Showing 5 of 5 references.

Isolation 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.

Gorny2003 Miroslaw K. Gorny and Susan Zolla-Pazner. Human Monoclonal Antibodies that Neutralize HIV-1. In Bette T. M. Korber and et. al., editors, HIV Immunology and HIV/SIV Vaccine Databases 2003. pages 37--51. Los Alamos National Laboratory, Theoretical Biology \& Biophysics, Los Alamos, N.M., 2004. URL: http://www.hiv.lanl.gov/content/immunology/pdf/2003/zolla-pazner_article.pdf. LA-UR 04-8162. Show all entries for this 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.