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Matheson, N.J.* ; Sumner, J.* ; Wals, K.* ; Rapiteanu, R.* ; Weekes, M.P.* ; Vigan, R.* ; Weinelt, J.* ; Schindler, M. ; Antrobus, R.* ; Costa, A.S.H.* ; Frezza, C.* ; Clish, C.B.* ; Neil, S.J.D.* ; Lehner, P.J.*

Cell surface proteomic map of HIV infection reveals antagonism of amino acid metabolism by Vpu and Nef.

Cell Host Microbe 18, 409-423 (2015)
Verlagsversion DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
ISSN (print) / ISBN 1931-3128
e-ISSN 1934-6069
Zeitschrift Cell Host & Microbe
Quellenangaben Band: 18, Heft: 4, Seiten: 409-423 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Virology (VIRO)