The Library
A bipartite structural organization defines the SERINC family of HIV-1 restriction factors
Tools
Tools
Tools
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
|
PDF
WRAP-bipartite-structural-organization-defines-SERINC-family-HIV-1-restriction-factors-Stansfeld-2019.pdf - Accepted Version - Requires a PDF viewer. Download (15Mb) | Preview |
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 | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Subjects: | Q Science > QL Zoology Q Science > QP Physiology Q Science > QR Microbiology |
|||||||||||||||||||||||||||||||||
| Divisions: | Faculty of 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: |
|
|||||||||||||||||||||||||||||||||
| Date of first compliant deposit: | 3 December 2019 | |||||||||||||||||||||||||||||||||
| 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: |
|
|||||||||||||||||||||||||||||||||
| Related URLs: |
Request changes or add full text files to a record
Repository staff actions (login required)
 |
View Item |
Downloads
Downloads per month over past year
