The structure and flexibility of conical HIV-1 capsids determined within intact virions

Author:

Mattei Simone12,Glass Bärbel3,Hagen Wim J. H.1,Kräusslich Hans-Georg23,Briggs John A. G.12

Affiliation:

1. Structural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.

2. Molecular Medicine Partnership Unit, European Molecular Biology Laboratory–Universitätsklinikum Heidelberg, Heidelberg, Germany.

3. Department of Infectious Diseases, Virology, Universitätsklinikum Heidelberg, Im Neuenheimer Feld 324, 69120 Heidelberg, Germany.

Abstract

Structural insights into capsid flexibility Viral capsids are protein structures that enclose the genetic material of viruses. Previous structural studies of the HIV-1 capsid have relied on recombinant, cross-linked, or mutant capsid proteins. Mattei et al. now report subnanometer-resolution cryo–electron tomography structures of the HIV-1 capsid from intact virions. These structures confirm the hollow cone shape of the capsid and allow for the specific placement of each individual capsid hexamer and pentamer within the lattice structure. The structures also reveal the flexible nature of the capsid, which likely helps it to accommodate interactions with host cell factors. Science , this issue p. 1434

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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