Tsg101 interacts with herpes simplex virus 1 VP1/2 and is a substrate of VP1/2 ubiquitin-specific protease domain activity.
Ubiquitination/deubiquitination of key factors represent crucial steps in the biogenesis of multivesicular body (MVB) and sorting of transmembrane proteins. We and others previously demonstrated that MVB is involved in herpes simplex virus 1 (HSV-1) envelopment and budding. Here, we report that the HSV-1 large tegument protein, VP1/2, interacts with and regulates the ubiquitination of Tsg101, a cellular protein essential in MVB formation, thus identifying the first cellular substrate of a herpesviral deubiquitinating enzyme.
Department of Molecular Medicine, University of Padova, Padova, Italy.
Martina
M
Caduco
Alessandra
A
Comin
Marta
M
Toffoletto
Denis
D
Munegato
Elena
E
Sartori
Michele
M
Celestino
Cristiano
C
Salata
Cristina
C
Parolin
Giorgio
G
Palù
Arianna
A
Calistri
D002460:Cell Line; D004268:DNA-Binding Proteins / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism*; D018259:Herpesvirus 1, Human / Q000472:pathogenicity*; D054884:Host-Pathogen Interactions; D006801:Humans; D014157:Transcription Factors / Q000378:metabolism*; D064570:Ubiquitin-Specific Proteases; D014764:Viral Proteins / Q000378:metabolism*; D000099177:Tsg101 Protein
D004268:DNA-Binding Proteins; D010450:Endopeptidases; D056827:Endosomal Sorting Complexes Required for Transport; D014157:Transcription Factors; D064570:Ubiquitin-Specific Proteases; D014764:Viral Proteins; D000099177:Tsg101 Protein; C078035:UL36 protein, Human herpesvirus 1