Maturation of the matrix and viral membrane of HIV-1

Author:

Qu Kun123ORCID,Ke Zunlong14ORCID,Zila Vojtech14ORCID,Anders-Össwein Maria4,Glass Bärbel24ORCID,Mücksch Frauke4ORCID,Müller Rainer35ORCID,Schultz Carsten356ORCID,Müller Barbara124ORCID,Kräusslich Hans-Georg13457ORCID,Briggs John A. G.1234ORCID

Affiliation:

1. Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, CB2 0QH Cambridge, UK.

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

3. Molecular Medicine Partnership Unit, European Molecular Biology Laboratory and Universitätsklinikum Heidelberg, 69117 Heidelberg, Germany.

4. Department of Infectious Diseases, Virology, Universitätsklinikum Heidelberg, 69120 Heidelberg, Germany.

5. Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.

6. Department of Chemical Physiology and Biochemistry, Oregon Health & Science University, Portland, OR 97239, USA.

7. German Center for Infection Research, Heidelberg, Germany.

Abstract

Structural changes in HIV maturation Nascent HIV particles assemble at the plasma membrane of an infected cell and bud into a membrane-enveloped, immature virion. Assembly and budding are driven by a polyprotein called Gag, which consists of a matrix domain (MA) that is recruited to the plasma membrane, a capsid domain (CA) responsible for self-assembly, and a nucleocapsid domain (NC) that recruits the viral RNA genome. Gag cleavage results in a structural rearrangement that produces the mature virion. Qu et al . imaged mature and immature HIV particles by electron tomography and focused in on the MA domain (see the Perspective by Hikichi and Freed). They found that MA rearranges between two distinct hexameric lattices, and mature MA modulates the viral membrane by binding to a membrane lipid. This finding suggests that MA may play functional roles in the mature virion. —VV

Funder

National Institutes of Health

H2020 European Research Council

European Molecular Biology Laboratory

Medical Research Council

Deutsche Forschungsgemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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