Journal
BIOCHEMICAL JOURNAL
Volume 431, Issue -, Pages 227-235Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20100558
Keywords
Epstein-Barr virus (EBV); ganciclovir; herpesvirus; phosphorylation; protein kinase
Categories
Funding
- National Institutes of Health [R21-AI072221]
- Deutsche Forschungsgemeinschaft [SFB 796/C3]
Ask authors/readers for more resources
A sole EBV (Epstein-Barr virus)-encoded protein kinase (EBV-PK) (the BGLF4 eerie product) plays important roles in viral infection. Although a number of targets of this protein have been identified, the kinase itself remains lamely unstudied with regard to its enzymology and structure In the present study. site-directed mutagenesis has been employed to generate mutations targeting residues involved in nuclear localization of the EBV-PK. core residues in subdomain III of the protein kinase domain conserved in most protein kinases or residues in subdomain VIa conserved only within the HPK (herpesvirus-encoded protein kinase) group Deletion of amino acids 389-391 resulted in exclusive cytoplasmic localization of the protein, indicating the involvement of this region in nuclear translocation of the EBV-PK Mutations at the amino acids Glu(113) (core component). Phe(175) Leu(178), Phe(184), Leu(185) and Asn(186) (conserved n HPKs) resulted in loss of EBV-PK autophosphorylation, protein substrate [EBV EA-D (early antigen diffused)] phosphorylation. and ability to facilitate ganciclovir phosphorylation. These results reiterate the unique features of this group of kinases and present an opportunity for designing more specific antiviral compounds
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available