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Vaccinology

A sweet cleft in HIV's armour

Nature volume 480, pages 324–325 (2011)Cite this article

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The structure of an antibody that potently neutralizes a wide range of HIV-1 strains, together with a minimal antigen mimic, is an advance towards the design of vaccines that may elicit protective responses. See Article p.336

The glycoproteins on the surface envelope of HIV-1 are essential for viral attachment to, and entry into, appropriate host cells. Antibodies that bind tightly to functional envelope glycoproteins neutralize virus infectivity and can protect against infection in vivo1. HIV-1 has, in turn, evolved various defence mechanisms against antibody neutralization, most prominent among which are amino-acid sequence variation and the masking of otherwise vulnerable regions on the envelope glycoproteins with sugars called glycans2. Most such immune-evasion measures have minimal effect on virus infectivity, but there are certain 'sites of vulnerability' on the envelope glycoproteins that the virus must keep relatively conserved and exposed to maintain function. In this issue, McLellan et al.3 define a new site of vulnerability on the HIV-1 surface glycoprotein gp120 by solving the atomic structure of a monoclonal antibody, PG9, in complex with a minimal antigenic mimic of gp120 (see page 336).

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Figure 1: Zooming in on the PG9–HIV-1 interaction.

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  1. Quentin J. Sattentau is in the Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.,

    Quentin J. Sattentau

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  1. Quentin J. Sattentau
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Correspondence to Quentin J. Sattentau.

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Sattentau, Q. A sweet cleft in HIV's armour. Nature 480, 324–325 (2011). https://doi.org/10.1038/480324a

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