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Gammaherpesviral Tegument Proteins, PML-Nuclear Bodies and the Ubiquitin-Proteasome System.
Full, Florian; Hahn, Alexander S; Großkopf, Anna K; Ensser, Armin.
Afiliación
  • Full F; Institute for Clinical and Molecular Virology, University Hospital Erlangen, Friedrich Alexander University Erlangen-Nuremberg, 91054 Erlangen, Germany. Florian.Full@uk-erlangen.de.
  • Hahn AS; Nachwuchsgruppe Herpesviren, Deutsches Primatenzentrum-Leibniz-Institut für Primatenforschung, 37077 Göttingen, Germany. AHahn@dpz.eu.
  • Großkopf AK; Nachwuchsgruppe Herpesviren, Deutsches Primatenzentrum-Leibniz-Institut für Primatenforschung, 37077 Göttingen, Germany. AGrosskopf@dpz.eu.
  • Ensser A; Institute for Clinical and Molecular Virology, University Hospital Erlangen, Friedrich Alexander University Erlangen-Nuremberg, 91054 Erlangen, Germany. armin.ensser@fau.de.
Viruses ; 9(10)2017 10 21.
Article en En | MEDLINE | ID: mdl-29065450
Gammaherpesviruses like Epstein-Barr virus (EBV) and Kaposi's sarcoma-associated herpesvirus (KSHV) subvert the ubiquitin proteasome system for their own benefit in order to facilitate viral gene expression and replication. In particular, viral tegument proteins that share sequence homology to the formylglycineamide ribonucleotide amidotransferase (FGARAT, or PFAS), an enzyme in the cellular purine biosynthesis, are important for disrupting the intrinsic antiviral response associated with Promyelocytic Leukemia (PML) protein-associated nuclear bodies (PML-NBs) by proteasome-dependent and independent mechanisms. In addition, all herpesviruses encode for a potent ubiquitin protease that can efficiently remove ubiquitin chains from proteins and thereby interfere with several different cellular pathways. In this review, we discuss mechanisms and functional consequences of virus-induced ubiquitination and deubiquitination for early events in gammaherpesviral infection.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Herpesvirus Humano 8 / Ubiquitina / Complejo de la Endopetidasa Proteasomal / Interacciones Huésped-Patógeno / Proteína de la Leucemia Promielocítica Límite: Animals / Humans Idioma: En Revista: Viruses Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Herpesvirus Humano 8 / Ubiquitina / Complejo de la Endopetidasa Proteasomal / Interacciones Huésped-Patógeno / Proteína de la Leucemia Promielocítica Límite: Animals / Humans Idioma: En Revista: Viruses Año: 2017 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Suiza