z-logo
open-access-imgOpen Access
Maturation of the matrix and viral membrane of HIV-1
Author(s) -
Kun Qu,
Zunlong Ke,
Vojtěch Žíla,
Maria AndersÖsswein,
Bärbel Glass,
Frauke Mücksch,
Rainer Müller,
Carsten Schultz,
Bárbara Müller,
HansGeorg Kräusslich,
John A. G. Briggs
Publication year - 2021
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abe6821
Subject(s) - human immunodeficiency virus (hiv) , matrix (chemical analysis) , virology , viral matrix protein , membrane , chemistry , biology , virus , biochemistry , chromatography
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. Quet 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

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom