Publikationsdatenbank

A herpesvirus ubiquitin-specific protease is critical for efficient T cell lymphoma formation (2007)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Jarosinski, Keith

Kattenhorn, Lisa

Kaufer, Benedikt (WE 5)

Ploegh, Hidde

Osterrieder, Klaus (WE 5)

Quelle

Proceedings of the National Academy of Sciences of the United States of America

Bandzählung: 104

Heftzählung: 50

Seiten: 20025 – 20030

ISSN: 1091-6490

Sprache

Englisch

Verweise

URL (Volltext): https://pubmed.ncbi.nlm.nih.gov/18056809/

DOI: 10.1073/pnas.0706295104

Pubmed: 18056809

Kontakt

Institut für Virologie

Robert-von-Ostertag-Str. 7-13
14163 Berlin
+49 30 838 51833
virologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

The herpesvirus ubiquitin-specific protease (USP) family, whose founding member was discovered as a protease domain embedded in the large tegument protein of herpes simplex virus 1 (HSV-1), is conserved across all members of the Herpesviridae. Whether this conservation is indicative of an essential function of the enzyme in vivo has not yet been established. As reported here, USP activity is conserved in Marek's disease virus (MDV), a tumorigenic alphaherpesvirus. A single amino acid substitution that abolishes the USP activity of the MDV large tegument protein diminishes MDV replication in vivo, and severely limits the oncogenic potential of the virus. Expression of the USP transcripts in MDV-transformed cell lines further substantiates this hypothesis. The herpesvirus USP thus appears to be required not only to maintain a foothold in the immunocompetent host, but also to contribute to malignant outgrowths.