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https://doi.org/10.1126/science.abe6821
Title: | Maturation of the matrix and viral membrane of HIV-1 | Authors: | Qu, Kun Ke, Zunlong Zila, Vojtech Anders-Oesswein, Maria Glass, Barbel Muecksch, Frauke Mueller, Rainer Schultz, Carsten Mueller, Barbara Kraeusslich, Hans-Georg Briggs, John AG |
Keywords: | Science & Technology Multidisciplinary Sciences Science & Technology - Other Topics IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE INCORPORATION PLASMA-MEMBRANE BINDING PROTEIN RETROVIRUS PHOSPHATIDYLINOSITOL-(4,5)-BISPHOSPHATE VISUALIZATION RESOLUTION FUSION |
Issue Date: | 6-Aug-2021 | Publisher: | AMER ASSOC ADVANCEMENT SCIENCE | Citation: | Qu, Kun, Ke, Zunlong, Zila, Vojtech, Anders-Oesswein, Maria, Glass, Barbel, Muecksch, Frauke, Mueller, Rainer, Schultz, Carsten, Mueller, Barbara, Kraeusslich, Hans-Georg, Briggs, John AG (2021-08-06). Maturation of the matrix and viral membrane of HIV-1. SCIENCE 373 (6555) : 700-704. ScholarBank@NUS Repository. https://doi.org/10.1126/science.abe6821 | 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. | Source Title: | SCIENCE | URI: | https://scholarbank.nus.edu.sg/handle/10635/247693 | ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.abe6821 |
Appears in Collections: | Staff Publications Elements |
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