Analysis of a Clonal Lineage of HIV-1 Envelope V2/V3 Conformational Epitope-Specific Broadly Neutralizing Antibodies and Their Inferred Unmutated Common Ancestors

Mattia Bonsignori(Duke Medical Center), Kwan-Ki Hwang(Duke Medical Center), Xi Chen(Duke Medical Center), Chun-Yen Tsao(Duke Medical Center), Lynn Morris(National Institute for Communicable Diseases), Elin S. Gray(National Institute for Communicable Diseases), Dawn J. Marshall(Duke Medical Center), John A. Crump(Duke University), Saidi Kapiga(London School of Hygiene & Tropical Medicine), Noel E. Sam(Kilimanjaro Christian Medical Centre), Faruk Sinangil(Global Solutions for Infectious Diseases), Marie Pancera, Yang Yongping, Baoshan Zhang, Jiang Zhu, Peter D. Kwong, Sijy O’Dell, John R. Mascola, Lan Wu, Gary J. Nabel, Sanjay Phogat(International AIDS Vaccine Initiative), Michael S. Seaman(Beth Israel Deaconess Medical Center), John F. Whitesides(Duke Medical Center), M. Anthony Moody(Duke Medical Center), Garnett Kelsoe(Duke Medical Center), Xinzhen Yang(Beth Israel Deaconess Medical Center), Joseph Sodroski(Dana-Farber Cancer Institute), George M. Shaw(University of Alabama at Birmingham), David C. Montefiori(Duke Medical Center), Thomas B. Kepler(Duke Medical Center), Georgia D. Tomaras(Duke Medical Center), S. Munir Alam(Duke Medical Center), Hua-Xin Liao(Duke Medical Center), Barton F. Haynes(Duke Medical Center)
Journal of Virology
July 28, 2011
Cited by 438Open Access
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Abstract

V2/V3 conformational epitope antibodies that broadly neutralize HIV-1 (PG9 and PG16) have been recently described. Since an elicitation of previously known broadly neutralizing antibodies has proven elusive, the induction of antibodies with such specificity is an important goal for HIV-1 vaccine development. A critical question is which immunogens and vaccine formulations might be used to trigger and drive the development of memory B cell precursors with V2/V3 conformational epitope specificity. In this paper we identified a clonal lineage of four V2/V3 conformational epitope broadly neutralizing antibodies (CH01 to CH04) from an African HIV-1-infected broad neutralizer and inferred their common reverted unmutated ancestor (RUA) antibodies. While conformational epitope antibodies rarely bind recombinant Env monomers, a screen of 32 recombinant envelopes for binding to the CH01 to CH04 antibodies showed monoclonal antibody (MAb) binding to the E.A244 gp120 Env and to chronic Env AE.CM243; MAbs CH01 and CH02 also bound to transmitted/founder Env B.9021. CH01 to CH04 neutralized 38% to 49% of a panel of 91 HIV-1 tier 2 pseudoviruses, while the RUAs neutralized only 16% of HIV-1 isolates. Although the reverted unmutated ancestors showed restricted neutralizing activity, they retained the ability to bind to the E.A244 gp120 HIV-1 envelope with an affinity predicted to trigger B cell development. Thus, E.A244, B.9021, and AE.CM243 Envs are three potential immunogen candidates for studies aimed at defining strategies to induce V2/V3 conformational epitope-specific antibodies.


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