Major tegument protein VP8 of bovine herpesvirus 1 is phosphorylated by viral US3 and cellular CK2 protein kinases

• Published in: Journal of general virology Vol. 90; no. 12; pp. 2829 - 2839
• Main Authors: Labiuk, Shaunivan L, Babiuk, Lorne A, Van Drunen Littel-van den Hurk, Sylvia
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.12.2009; Society for General Microbiology
• Subjects: Animals; autophosphorylation; Benzimidazoles - pharmacology; Biological and medical sciences; Bovine alphaherpesvirus 1; Bovine herpesvirus 1; Capsid Proteins - metabolism; Casein Kinase II - antagonists & inhibitors; Casein Kinase II - metabolism; Cattle; Cell Line; cell lines; Chlorocebus aethiops; COS Cells; cytopathogenicity; enzyme activity; Fundamental and applied biological sciences. Psychology; Herpesvirus 1, Bovine - genetics; Herpesvirus 1, Bovine - growth & development; Herpesvirus 1, Bovine - metabolism; host-pathogen relationships; Immunoprecipitation; infection; Kidney - cytology; Mass Spectrometry; Microbiology; Miscellaneous; Phosphorylation; protein kinases; protein phosphorylation; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; tegument protein; viral proteins; Viral Proteins - genetics; Viral Proteins - metabolism; Virology; VP8 protein; Virus; Phosphorylation; Microbiology; Enzyme; Herpesviridae; Transferases; Non-specific serine/threonine protein kinase; Alphaherpesvirinae; Bovine herpesvirus 1; Veterinary; In vitro; Protein

The UL47 gene product, VP8, is one of the major tegument proteins of bovine herpesvirus 1 (BoHV-1) and is subject to phosphorylation. Analysis of protein bands co-immunoprecipitated with VP8 from BoHV-1-infected cells by mass spectroscopy suggested that VP8 interacts with two protein kinases: cellul...