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A bipartite structural organization defines the SERINC family of HIV-1 restriction factors
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Pye, Valerie E., Rosa, Annachiara, Bertelli, Cinzia, Struwe, Weston B., Maslen, Sarah L., Corey, Robin A., Liko, Idlir, Hassall, Mark, Mattiuzzo, Giada, Ballandras-Colas, Allison, Nans, Andrea, Takeuchi, Yasuhiro, Stansfeld, Phillip J., Skehel, J. Mark, Robinson, Carol V., Pizzato, Massimo and Cherepanov, Peter (2020) A bipartite structural organization defines the SERINC family of HIV-1 restriction factors. Nature Structural & Molecular Biology, 27 . pp. 78-83. doi:10.1038/s41594-019-0357-0 ISSN 1545-9993.
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Official URL: http://dx.doi.org/10.1038/s41594-019-0357-0
Abstract
The human integral membrane protein SERINC5 potently restricts HIV-1 infectivity and sensitizes the virus to antibody-mediated neutralization. Here, using cryo-EM, we determine the structures of human SERINC5 and its orthologue from Drosophila melanogaster at subnanometer and near-atomic resolution, respectively. The structures reveal a novel fold comprised of ten transmembrane helices organized into two subdomains and bisected by a long diagonal helix. A lipid binding groove and clusters of conserved residues highlight potential functional sites. A structure-based mutagenesis scan identified surface-exposed regions and the interface between the subdomains of SERINC5 as critical for HIV-1-restriction activity. The same regions are also important for viral sensitization to neutralizing antibodies, directly linking the antiviral activity of SERINC5 with remodeling of the HIV-1 envelope glycoprotein.
Item Type: | Journal Article | |||||||||||||||||||||||||||||||||
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Subjects: | Q Science > QL Zoology Q Science > QP Physiology Q Science > QR Microbiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | |||||||||||||||||||||||||||||||||
Library of Congress Subject Headings (LCSH): | Membrane proteins, Drosophila melanogaster, Glycoproteins, HIV (Viruses) | |||||||||||||||||||||||||||||||||
Journal or Publication Title: | Nature Structural & Molecular Biology | |||||||||||||||||||||||||||||||||
Publisher: | Nature Publishing Group | |||||||||||||||||||||||||||||||||
ISSN: | 1545-9993 | |||||||||||||||||||||||||||||||||
Official Date: | 6 January 2020 | |||||||||||||||||||||||||||||||||
Dates: |
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Volume: | 27 | |||||||||||||||||||||||||||||||||
Page Range: | pp. 78-83 | |||||||||||||||||||||||||||||||||
DOI: | 10.1038/s41594-019-0357-0 | |||||||||||||||||||||||||||||||||
Status: | Peer Reviewed | |||||||||||||||||||||||||||||||||
Publication Status: | Published | |||||||||||||||||||||||||||||||||
Access rights to Published version: | Restricted or Subscription Access | |||||||||||||||||||||||||||||||||
Date of first compliant deposit: | 3 December 2019 | |||||||||||||||||||||||||||||||||
Date of first compliant Open Access: | 6 July 2020 | |||||||||||||||||||||||||||||||||
RIOXX Funder/Project Grant: |
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