NDLI: A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope

Content Provider	PubMed Central
Author	Miller, Michael D. Romas, Geleziunas Bianchi, Elisabetta Lennard, Simon Renee, Hrin Zhang, Hangchun Lu, Meiqing An, Zhiqiang Paolo, Ingallinella Finotto, Marco Mattu, Marco Finnefrock, Adam C. Bramhill, David Cook, James Eckert, Debra M. Hampton, Richard Patel, Mayuri Stephen, Jarantow Joyce, Joseph Ciliberto, Gennaro Cortese, Riccardo Lu, Ping Strohl, William Schleif, William Michael, Mcelhaugh Lane, Steven Lloyd, Christopher Lowe, David Osbourn, Jane Vaughan, Tristan Emini, Emilio Barbato, Gaetano Kim, Peter S. Hazuda, Daria J. Shiver, John W. Pessi, Antonello
Copyright Year	2005
Abstract	HIV-1 entry into cells is mediated by the envelope glycoprotein receptor-binding (gp120) and membrane fusion-promoting (gp41) subunits. The gp41 heptad repeat 1 (HR1) domain is the molecular target of the fusion-inhibitor drug enfuvirtide (T20). The HR1 sequence is highly conserved and therefore considered an attractive target for vaccine development, but it is unknown whether antibodies can access HR1. Herein, we use gp41-based peptides to select a human antibody, 5H/I1-BMV-D5 (D5), that binds to HR1 and inhibits the assembly of fusion intermediates in vitro. D5 inhibits the replication of diverse HIV-1 clinical isolates and therefore represents a previously unknown example of a crossneutralizing IgG selected by binding to designed antigens. NMR studies and functional analyses map the D5-binding site to a previously identified hydrophobic pocket situated in the HR1 groove. This hydrophobic pocket was proposed as a drug target and subsequently identified as a common binding site for peptide and peptidomimetic fusion inhibitors. The finding that the D5 fusion-inhibitory antibody shares the same binding site suggests that the hydrophobic pocket is a “hot spot” for fusion inhibition and an ideal target on which to focus a vaccine-elicited antibody response. Our data provide a structural framework for the design of new immunogens and therapeutic antibodies with crossneutralizing potential.
Related Links	http://dx.doi.org/10.1073/pnas.0506927102
Starting Page	14759
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	41
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-10-11
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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