JVI Accepts, published online ahead of print on 27 January 2010

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J. Virol. doi:10.1128/JVI.02617-09
Copyright (c) 2010, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Quaternary epitope specificities of anti-HIV-1 neutralizing antibodies generated in rhesus macaques infected by the simian/human immunodeficiency virus SHIV_SF162P4

James E Robinson^*, Kelly Franco, Debra Holton Elliott, Mary Jane Maher, Ashley Reyna, David Montefiori, Susan Zolla-Pazner, Miroslaw K. Gorny, Zane Kraft, and Leonidas Stamatatos^*

Department of Pediatrics, Tulane University Medical Center, New Orleans, Louisiana 70012; Duke University Medical Center, Durham, NC 27710; Seattle Biomedical Research Institute, Seattle, Washington 98109; Department of Pathology, New York University Langone School of Medicine, New York, New York 10016; Research Center for AIDS and HIV Infection, Veterans Affairs Medical Center, New York, New York 10010; Department of Global Health, University of Washington, Seattle, Washington 98109

^* To whom correspondence should be addressed. Email: jrobinso{at}tulane.edu. leo.stamatatos{at}sbri.org.

Monoclonal antibodies (MAbs) that neutralize the human immunodeficiency virus type one (HIV-1) have been isolated from HIV-1 infected individuals or animals immunized with recombinant HIV-1 Envelope glycoprotein constructs (Env). The epitopes of these neutralizing antibodies (NAbs) were shown to be located on either the variable or conserved regions of the HIV-1 Env and to be linear or conformational. However, one neutralizing MAb, 2909, which was isolated from an HIV-1-infected subject, recognizes a more complex, quaternary epitope that is present on the virion-associated functional trimeric Env spike of the SF162 HIV-1 isolate. Here, we discuss the isolation of eleven anti-HIV NAbs isolated from three rhesus macaques infected with the simian/human immunodeficiency virus SHIV_SF162P4, and which also recognize quaternary epitopes. A detailed epitope mapping analysis of three of these rhesus antibodies revealed that their epitopes overlap that of the human MAb 2909. Despite this overall similarity in binding, however, differences in specific amino acid and glycosylation pattern requirements for MAb 2909 and the rhesus MAbs were identified. These results highlight similarities in the B cell responses of humans and macaques to structurally complex neutralization epitopes on related viruses, HIV-1 and SHIV.

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