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.
Copyright © 2021, American Association for the Advancement of Science.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Capsid / chemistry
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Capsid / physiology
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Electron Microscope Tomography
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HIV Antigens / chemistry*
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HIV Antigens / metabolism*
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HIV-1 / chemistry*
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HIV-1 / physiology*
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HIV-1 / ultrastructure
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Lipid Bilayers
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Membrane Lipids / metabolism
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Models, Molecular
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Protein Conformation
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Protein Domains
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Protein Structure, Secondary
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Viral Envelope / chemistry
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Viral Envelope / metabolism*
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Viral Envelope / ultrastructure
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Virion / chemistry
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Virion / physiology
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Virion / ultrastructure
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Virus Assembly
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env Gene Products, Human Immunodeficiency Virus / chemistry
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env Gene Products, Human Immunodeficiency Virus / metabolism
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gag Gene Products, Human Immunodeficiency Virus / chemistry*
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gag Gene Products, Human Immunodeficiency Virus / metabolism*
Substances
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HIV Antigens
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Lipid Bilayers
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Membrane Lipids
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env Gene Products, Human Immunodeficiency Virus
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gag Gene Products, Human Immunodeficiency Virus
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p17 protein, Human Immunodeficiency Virus Type 1