An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation

Author:

Schur Florian K. M.12,Obr Martin23,Hagen Wim J. H.1,Wan William1,Jakobi Arjen J.14,Kirkpatrick Joanna M.5,Sachse Carsten1,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.

4. Hamburg Unit c/o DESY (Deutsches Elektronen-Synchrotron), European Molecular Biology Laboratory, Notkestraße 85, 22607 Hamburg, Germany.

5. Proteomics Core Facility, European Molecular Biology Laboratory, Meyerhofstraße 1, 69117 Heidelberg, Germany.

Abstract

Maturation and inhibition of HIV-1 HIV-1 undergoes a two-step assembly process controlled largely by a single region of its Gag protein. Schur et al. determined a complete atomic model for this region within an assembled Gag protein lattice using cryo-electron tomography together with subtomogram averaging. Amino acids from different parts of multiple Gag molecules come together to form an intricate network of interactions that drive HIV-1 assembly. The final step of maturation into the infectious HIV-1 virus is controlled by structural changes in Gag that alter the accessibility of the final cleavage site to the viral protease. Science , this issue p. 506

Funder

Deutsche Forschungsgemeinschaft

European Molecular Biology Laboratory (EMBL)

Chica und Heinz Schaller Stiftung

European Molecular Biology Organization Long-Term Fellowship

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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