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  Maturation of the matrix and viral membrane of HIV-1

Qu, K., Ke, Z. L., Zila, V., Anders-Osswein, M., Glass, B., Mucksch, F., et al. (2021). Maturation of the matrix and viral membrane of HIV-1. Science, 373(6555), 700-704. doi:10.1126/science.abe6821.

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Qu, K., Author
Ke, Z. L., Author
Zila, V., Author
Anders-Osswein, M., Author
Glass, B., Author
Mucksch, F., Author
Muller, R., Author
Schultz, C., Author
Muller, B., Author
Krausslich, H. G., Author
Briggs, John A. G.1, 2, Author           
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              
2European Molecular Biology Laboratory, External Organizations, Heidelberg, DE, ou_3346677              

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Free keywords: immunodeficiency-virus type-1 envelope incorporation plasma-membrane binding protein retrovirus phosphatidylinositol-(4,5)-bisphosphate visualization resolution fusion Science & Technology - Other Topics
 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.

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Language(s): eng - English
 Dates: 2021
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000681722700044
DOI: 10.1126/science.abe6821
ISSN: 0036-8075
 Degree: -

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Title: Science
  Alternative Title : Science
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 373 (6555) Sequence Number: - Start / End Page: 700 - 704 Identifier: -