A bipartite structural organization defines the SERINC family of HIV-1 restriction factors-Reference-Cited by-同舟云学术

A bipartite structural organization defines the SERINC family of HIV-1 restriction factors

Published:2020-01 Issue:1 Volume:27 Page:78-83
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Pye Valerie E.^ORCID,Rosa Annachiara,Bertelli Cinzia,Struwe Weston B.,Maslen Sarah L.,Corey Robin,Liko Idlir,Hassall Mark,Mattiuzzo Giada^ORCID,Ballandras-Colas Allison,Nans Andrea^ORCID,Takeuchi Yasuhiro,Stansfeld Phillip J.^ORCID,Skehel J. Mark,Robinson Carol V.,Pizzato Massimo^ORCID,Cherepanov Peter^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/s41594-019-0357-0.pdf

Reference58 articles.

1. Duggal, N. K. & Emerman, M. Evolutionary conflicts between viruses and restriction factors shape immunity. Nat. Rev. Immunol. 12, 687–695 (2012).

2. Rosa, A. et al. HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation. Nature 526, 212–217 (2015).

3. Usami, Y., Wu, Y. & Gottlinger, H. G. SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef. Nature 526, 218–223 (2015).

4. Chande, A. et al. S2 from equine infectious anemia virus is an infectivity factor which counteracts the retroviral inhibitors SERINC5 and SERINC3. Proc. Natl Acad. Sci. USA 113, 13197–13202 (2016).

5. Ahmad, I. et al. The retroviral accessory proteins S2, Nef, and glycoMA use similar mechanisms for antagonizing the host restriction factor SERINC5. J. Biol. Chem. 294, 7013–7024 (2019).

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