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Status: Bibliographieeintrag

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Verfasst von:Trautz, Birthe [VerfasserIn]   i
 Olschowski, Hannah [VerfasserIn]   i
 Lüchtenborg, Christian [VerfasserIn]   i
 Pierini, Virginia [VerfasserIn]   i
 Glass, Bärbel [VerfasserIn]   i
 Kräusslich, Hans-Georg [VerfasserIn]   i
 Ruggieri, Alessia [VerfasserIn]   i
 Brügger, Britta [VerfasserIn]   i
 Fackler, Oliver Till [VerfasserIn]   i
Titel:The host-cell restriction factor SERINC5 restricts HIV-1 infectivity without altering the lipid composition and organization of viral particles
Verf.angabe:Birthe Trautz, Hannah Wiedemann, Christian Lüchtenborg, Virginia Pierini, Jan Kranich, Bärbel Glass, Hans-Georg Kräusslich, Thomas Brocker, Massimo Pizzato, Alessia Ruggieri, Britta Brügger, and Oliver T. Fackler
E-Jahr:2017
Jahr:June 28, 2017
Umfang:12 S.
Fussnoten:Gesehen am 06.08.2018
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : Soc., 1905
Jahr Quelle:2017
Band/Heft Quelle:292(2017), 33, Seite 13702-13713
ISSN Quelle:1083-351X
Abstract:The host-cell restriction factor SERINC5 potently suppresses the infectivity of HIV, type 1 (HIV-1) particles, and is counteracted by the viral pathogenesis factor Nef. However, the molecular mechanism by which SERINC5 restricts HIV-1 particle infectivity is still unclear. Because SERINC proteins have been suggested to facilitate the incorporation of serine during the biosynthesis of membrane lipids and because lipid composition of HIV particles is a major determinant of the infectious potential of the particles, we tested whether SERINC5-mediated restriction of HIV particle infectivity involves alterations of membrane lipid composition. We produced and purified HIV-1 particles from SERINC5293T cells with very low endogenous SERINC5 levels under conditions in which ectopically expressed SERINC5 restricts HIV-1 infectivity and is antagonized by Nef and analyzed both virions and producer cells with quantitative lipid MS. SERINC5 restriction and Nef antagonism were not associated with significant alterations in steady-state lipid composition of producer cells and HIV particles. Sphingosine metabolism kinetics were also unaltered by SERINC5 expression. Moreover, the levels of phosphatidylserine on the surface of HIV-1 particles, which may trigger uptake into non-productive internalization pathways in target cells, did not change upon expression of SERINC5 or Nef. Finally, saturating the phosphatidylserine-binding sites on HIV target cells did not affect SERINC5 restriction or Nef antagonism. These results demonstrate that the restriction of HIV-1 particle infectivity by SERINC5 does not depend on alterations in lipid composition and organization of HIV-1 particles and suggest that channeling serine into lipid biosynthesis may not be a cardinal cellular function of SERINC5.
DOI:doi:10.1074/jbc.M117.797332
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Kostenfrei: Volltext ; Verlag: http://dx.doi.org/10.1074/jbc.M117.797332
 Kostenfrei: Volltext: http://www.jbc.org/content/292/33/13702
 DOI: https://doi.org/10.1074/jbc.M117.797332
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:host cell restriction factor
 host-pathogen interaction
 human immunodeficiency virus (HIV)
 infectious disease
 lipid
 lipid composition
 Nef
 SERINC5
 viral protein
K10plus-PPN:157827141X
Verknüpfungen:→ Zeitschrift

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