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Published February 2016 | Published
Journal Article Open

Structure of an HIV-2 gp120 in complex with CD4

Davenport, Yunji W.
West, Anthony P.
Bjorkman, Pamela J. ORCID icon
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Abstract

HIV-2 is a nonpandemic form of the virus causing AIDS, and the majority of HIV-2-infected patients exhibit long-term nonprogression. The HIV-1 and HIV-2 envelope glycoproteins, the sole targets of neutralizing antibodies, share 30 to 40% identity. As a first step in understanding the reduced pathogenicity of HIV-2, we solved a 3.0-Å structure of an HIV-2 gp120 bound to the host receptor CD4, which reveals structural similarity to HIV-1 gp120 despite divergence in amino acid sequence.

Additional Information

© 2015 American Society for Microbiology. Received 19 October 2015; Accepted 19 November 2015; Accepted manuscript posted online 25 November 2015. We thank Jost Vielmetter and the Caltech Protein Expression Center for assistance with protein expression, Jens Kaiser, Pavle Nikolovski, the Caltech Molecular Observatory, and the staff at Beamline 12-2 (SSRL) for assistance with crystallographic data collection, the developers of PHENIX, CCP4, and XDS software, and Robbie Joosten of PDB_REDO for assistance and advice concerning X-ray crystallography. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. This work was supported by Collaboration for AIDS Vaccine Discovery grants from the Bill and Melinda Gates Foundation (grants 1040753 and 1124068 to P.J.B.) and by the National Institute of Allergy and Infectious Diseases, NIH, grant HIVRAD P01 AI100148 (P.J.B.). The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

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