Maturation of the matrix and viral membrane of HIV-1

Copyright © 2021, American Association for the Advancement of Science..

Gag, the primary structural protein of HIV-1, is recruited to the plasma membrane for virus assembly by its matrix (MA) domain. Gag is subsequently cleaved into its component domains, causing structural maturation to repurpose the virion for cell entry. We determined the structure and arrangement of MA within immature and mature HIV-1 through cryo-electron tomography. We found that MA rearranges between two different hexameric lattices upon maturation. In mature HIV-1, a lipid extends out of the membrane to bind with a pocket in MA. Our data suggest that proteolytic maturation of HIV-1 not only assembles the viral capsid surrounding the genome but also repurposes the membrane-bound MA lattice for an entry or postentry function and results in the partial removal of up to 2500 lipids from the viral membrane.

Errataetall:

CommentIn: Science. 2021 Aug 6;373(6555):621-622. - PMID 34353938

Medienart:

E-Artikel

Erscheinungsjahr:

2021

Erschienen:

2021

Enthalten in:

Zur Gesamtaufnahme - volume:373

Enthalten in:

Science (New York, N.Y.) - 373(2021), 6555 vom: 06. Aug., Seite 700-704

Sprache:

Englisch

Beteiligte Personen:

Qu, Kun [VerfasserIn]
Ke, Zunlong [VerfasserIn]
Zila, Vojtech [VerfasserIn]
Anders-Össwein, Maria [VerfasserIn]
Glass, Bärbel [VerfasserIn]
Mücksch, Frauke [VerfasserIn]
Müller, Rainer [VerfasserIn]
Schultz, Carsten [VerfasserIn]
Müller, Barbara [VerfasserIn]
Kräusslich, Hans-Georg [VerfasserIn]
Briggs, John A G [VerfasserIn]

Links:

Volltext

Themen:

Env Gene Products, Human Immunodeficiency Virus
Gag Gene Products, Human Immunodeficiency Virus
HIV Antigens
Journal Article
Lipid Bilayers
Membrane Lipids
P17 protein, Human Immunodeficiency Virus Type 1
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Anmerkungen:

Date Completed 20.08.2021

Date Revised 07.02.2022

published: Print

CommentIn: Science. 2021 Aug 6;373(6555):621-622. - PMID 34353938

Citation Status MEDLINE

doi:

10.1126/science.abe6821

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM328982628