Abstract
Bovine herpesvirus 1 (BHV-1), an alphaherpesvirus, is a major pathogen that causes respiratory and reproductive infections. We observed tyrosine phosphorylation of a 95-kDa viral protein and dephosphorylation of 55- and 103-kDa cellular proteins during the course of BHV-1 infection. We demonstrated BHV-1 glycoprotein E (gE) to be the tyrosine phosphorylated viral protein by immunoprecipitation. Inhibition of phosphorylation of BHV-1 gE by tyrosine kinase inhibitors genistein and tyrphostin AG1478 substantially lowered the viral titer in Madin-Darby bovine kidney cells. The decrease in viral titer was directly proportional to the decrease in phosphorylation of the BHV-1 gE. Interestingly, these kinase inhibitors did not inhibit the replication of the BHV-1 gE deletion mutant virion (BHV- 1gEΔ3.1). Our findings suggest that the wild-type BHV-1, with a functional gE protein, uses a different pathway of signaling events than the BHV-1 gE deletion mutant in replication. Our results indicate that the tyrosine phosphorylation of the cytoplasmic tail of BHV-1 gE is an important post- translational modification of the functional protein. An application of this study may be the use of tyrosine kinase inhibitors in controlling the BHV-1 infection. (C) 2000 Academic Press.
Original language | English (US) |
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Pages (from-to) | 159-166 |
Number of pages | 8 |
Journal | Virology |
Volume | 268 |
Issue number | 1 |
DOIs | |
State | Published - Mar 1 2000 |
Externally published | Yes |
ASJC Scopus subject areas
- Virology