Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 346, Issue 2, Pages 577-588Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2004.11.064
Keywords
HIV; virus structure; tomography; electron cryomicroscopy; capsid
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Funding
- NIGMS NIH HHS [P01 GM66521, P01 GM066521] Funding Source: Medline
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While the structures of nearly every HIV-1 protein are known in atomic detail from X-ray crystallography and NMR spectroscopy, many questions remain about how the individual proteins are arranged in the mature infectious viral particle. Here, we report the three-dimensional structures of individual HIV-1 virus-like particles (VLPs) as obtained by electron cryotomography. These reconstructions revealed that while the structures and positions of the conical cores within each VLP were unique, they exhibited several surprisingly consistent features, including similarities in the size and shape of the wide end of the capsid (the base), uniform positioning of the base and other regions of the capsid 11 nm away from the envelope/MA layer, a cone angle that typically varied from 24degrees to 18degrees around the long axis of the cone, and an internal density (presumably part of the NC/RNA complex) cupped within the base. Multiple and nested capsids, were observed. These results support the fullerene cone model for the viral capsid, indicate that viral maturation involves a free re-organization of the capsid shell rather than a continuous condensation, imply that capsid assembly is both concentration-driven and template-driven, suggest that specific interactions exist between the capsid and the adjacent envelope/MA and NC/RNA layers, and show that a particular capsid shape is favored strongly in-vivo. (C) 2004 Elsevier Ltd. All rights reserved.
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