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Matheson, Nicholas J.; Sumner, Jonathan; Wals, Kim; Rapiteanu, Radu; Weekes, Michael P.; Vigan, Raphael; Weinelt, Julia; Schindler, Michael; Antrobus, Robin; Costa, Ana S.H.; Frezza, Christian; Clish, Clary B.; Neil, Stuart J.D.; Lehner, Paul J.
Cell host & microbe, 10/2015, Letnik: 18, Številka: 4Journal Article
Critical cell surface immunoreceptors downregulated during HIV infection have previously been identified using non-systematic, candidate approaches. To gain a comprehensive, unbiased overview of how HIV infection remodels the T cell surface, we took a distinct, systems-level, quantitative proteomic approach. >100 plasma membrane proteins, many without characterized immune functions, were downregulated during HIV infection. Host factors targeted by the viral accessory proteins Vpu or Nef included the amino acid transporter SNAT1 and the serine carriers SERINC3/5. We focused on SNAT1, a β-TrCP-dependent Vpu substrate. SNAT1 antagonism was acquired by Vpu variants from the lineage of SIVcpz/HIV-1 viruses responsible for pandemic AIDS. We found marked SNAT1 induction in activated primary human CD4+ T cells, and used Consumption and Release (CoRe) metabolomics to identify alanine as an endogenous SNAT1 substrate required for T cell mitogenesis. Downregulation of SNAT1 therefore defines a unique paradigm of HIV interference with immunometabolism. Display omitted •Unbiased global analysis of T cell surface proteome remodeling during HIV infection•>100 proteins downregulated, including Nef targets SERINC3/5 and Vpu target SNAT1•β-TrCP-dependent SNAT1 downregulation acquired by pandemic SIVcpz/HIV-1 viruses•Uptake of exogenous alanine by SNAT1 critical for primary CD4+ T cell mitogenesis Viruses manipulate host factors to enhance their replication. Matheson et al. use functional proteomics to analyze plasma membrane proteins downregulated during HIV-1 infection. Serine carriers SERINC3/5 and alanine transporter SNAT1 were identified as Nef and Vpu targets, respectively. Antagonism of SNAT1-mediated alanine transport enables viral interference with T cell immunometabolism
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in: SICRIS
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