Identification of host cell proteins which interact with herpes simplex virus type 1 tegument protein pUL37.
The herpes simplex virus type 1 (HSV-1) structural tegument protein pUL37, which is conserved across the Herpesviridae family, is known to be essential for secondary envelopment during the egress of viral particles. To shed light on additional roles of pUL37 during viral replication a yeast two-hybrid screen of a human brain cDNA library was undertaken. This screen identified ten host cell proteins as potential pUL37 interactors. One of the interactors, serine threonine kinase TAOK3, was subsequently confirmed to interact with pUL37 using an in vitro pulldown assay. Such host cell/pUL37 interactions provide further insights into the multifunctional role of this herpesviral tegument protein.
Centre for Virus Research, The Westmead Millennium Institute, The University of Sydney, Westmead, NSW, Australia.
Barbara J
BJ
Kelly
Eve
E
Diefenbach
Cornel
C
Fraefel
Russell J
RJ
Diefenbach
D001921:Brain / Q000378:metabolism* / Q000821:virology; D015723:Gene Library; D006561:Herpes Simplex / Q000378:metabolism*; D018259:Herpesvirus 1, Human / Q000378:metabolism / Q000502:physiology*; D054884:Host-Pathogen Interactions; D006801:Humans; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D020798:Two-Hybrid System Techniques; D015678:Viral Structural Proteins / Q000378:metabolism*; D014779:Virus Replication
C084763:UL37 protein, Human herpesvirus 1; D015678:Viral Structural Proteins; D017346:Protein Serine-Threonine Kinases