EMD-13088
Mature HIV-1 matrix structure
EMD-13088
Subtomogram averaging7.0 Å
Deposition: 15/06/2021
Map released: 18/08/2021
Last modified: 13/11/2024
Sample Organism:
Human immunodeficiency virus 1
Sample: Human immunodeficiency virus 1
Fitted models: 7ovr (Avg. Q-score: 0.245)
Deposition Authors: Qu K , Ke ZL, Zila V , Anders-Oesswein M, Glass B , Muecksch F, Mueller R, Schultz C , Mueller B, Kraeusslich HG, Briggs JAG
Sample: Human immunodeficiency virus 1
Fitted models: 7ovr (Avg. Q-score: 0.245)
Deposition Authors: Qu K , Ke ZL, Zila V , Anders-Oesswein M, Glass B , Muecksch F, Mueller R, Schultz C , Mueller B, Kraeusslich HG, Briggs JAG
Maturation of the matrix and viral membrane of HIV-1.
Qu K ,
Ke Z ,
Zila V ,
Anders-Osswein M,
Glass B ,
Mucksch F ,
Muller R ,
Schultz C ,
Muller B ,
Krausslich HG ,
Briggs JAG
(2021) Science , 373 , 700 - 704
(2021) Science , 373 , 700 - 704
Abstract:
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.
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.