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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

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Official URL: http://dx.doi.org/10.1038/s41594-019-0357-0

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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
Subjects: Q Science > QL Zoology
Q Science > QP Physiology
Q Science > QR Microbiology
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:
DateEvent
6 January 2020Published
2019Available
26 November 2019Accepted
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
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
208361/Z/17/ZWellcome Trusthttp://dx.doi.org/10.13039/100010269
MR/S009213/1[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
BB/P01948X/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/R002517/1 [BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/S003339/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
EP/R029407/1[EPSRC] Engineering and Physical Sciences Research Councilhttp://dx.doi.org/10.13039/501100000266
P50 AI150481National Institutes of Healthhttp://dx.doi.org/10.13039/100000002
FC001061Cancer Research UKhttp://dx.doi.org/10.13039/501100000289
FC001061[MRC] Medical Research Councilhttp://dx.doi.org/10.13039/501100000265
FC001061Wellcome Trusthttp://dx.doi.org/10.13039/100010269
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