TY - JOUR
T1 - Maturation of the matrix and viral membrane of HIV-1
AU - Qu, Kun
AU - Ke, Zunlong
AU - Zila, Vojtech
AU - Anders-Össwein, Maria
AU - Glass, Bärbel
AU - Mücksch, Frauke
AU - Müller, Rainer
AU - Schultz, Carsten
AU - Müller, Barbara
AU - Kräusslich, Hans Georg
AU - Briggs, John A.G.
N1 - Publisher Copyright:
© 2021 American Association for the Advancement of Science. All rights reserved.
PY - 2021/8/6
Y1 - 2021/8/6
N2 - 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.
AB - 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.
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U2 - 10.1126/science.abe6821
DO - 10.1126/science.abe6821
M3 - Article
C2 - 34353956
AN - SCOPUS:85112250283
SN - 0036-8075
VL - 373
SP - 700
EP - 704
JO - Science
JF - Science
IS - 6555
ER -