An N-Glycosylated Form of SERINC5 Is Specifically Incorporated into HIV-1 Virions.

Journal of Virology
Shilpi SharmaJohn Guatelli

Abstract

SERINC5 is an inhibitor of retroviral infectivity that is counteracted by viral proteins, including HIV-1 Nef. Inhibition of infectivity by SERINC5 is associated with its incorporation into virions. Nef counteracts this inhibition, presumably by removing SERINC5 from sites of virion assembly at the plasma membrane. While evaluating the virion incorporation of SERINC5, we observed that a relatively high molecular weight form was preferentially present in virions. We used various glycosidases to establish that virion-associated SERINC5 is modified by N-linked, complex glycans, whereas the majority of SERINC5 in cells is of relatively low molecular weight and is modified by high-mannose glycans. Sequence alignment of SERINC family proteins led us to identify a conserved N-glycosylation site, N294, in SERINC5. We mutated this site to evaluate its effect on glycosylation, the restrictive activity of SERINC5, and the sensitivity of SERINC5 to antagonism by Nef. Our results demonstrate that N294 is the major site of N-glycosylation in SERINC5. Although N-glycosylation was required neither for restrictive activity nor for sensitivity to Nef per se, we observed a decrease in the steady-state expression of glycosylation-deficient SERINC5...Continue Reading

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Citations

Oct 11, 2019·Journal of Virology·Vânia PassosChristine Goffinet
Jan 17, 2020·Journal of Virology·Charlotte A StonehamJohn Guatelli
Aug 17, 2020·Journal of Virology·Austin Featherstone, Christopher Aiken
Dec 20, 2018·The Journal of General Virology·Patrícia de Sousa-PereiraHanna-Mari Baldauf
Jul 16, 2020·MBio·Uddhav TimilsinaSpyridon Stavrou
Jul 5, 2019·Retrovirology·Elodie MaillerJuan S Bonifacino
Jan 8, 2020·Nature Structural & Molecular Biology·Valerie E PyePeter Cherepanov
Aug 14, 2020·The Journal of Biological Chemistry·Amanda E WardLukas K Tamm
Sep 3, 2020·The Journal of Biological Chemistry·Ryan P Staudt, Thomas E Smithgall

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