Thymidine kinase (TK) induced by varicella-zoster virus (VZV) was precipitated with ammonium sulphate and purified by Sephadex G-150, QAE-Sephadex and Blue Sepharose column chromatographies. The purified TK fraction also contained deoxycytidine kinase (dCK) activity and a 35 000 mol. wt. (35K) polypeptide as a major component. The TK and dCK activities were both neutralized by anti-VZV serum. Antiserum to an extract of cells infected with a bromodeoxyuridine (BUdR)-resistant mutant virus contained no antibody to the viral TK and dCK activities or to the 35K polypeptide. Antiserum to the purified viral TK fraction was prepared and absorbed with a lysate of BUdR-resistant mutant virus-infected cells. The resulting absorbed antiserum (anti-vTK serum) neutralized the viral activities of both TK and dCK, and specifically immunoprecipitated a 35K polypeptide from the lysate of parental virus-infected cells, but did not immunoprecipitate any detectable polypeptide from cells infected with BUdR-resistant mutant virus. Anti-vTK serum stained mainly the nuclei of cells infected with the parental virus strain, but did not stain those infected with BUdR-resistant mutant virus by an indirect fluorescent antibody test. These results suggest that the 35K polypeptide produced in VZV-infected cells is responsible for the viral TK and dCK activities, and that the TK and dCK are mainly localized in the nuclei of infected cells.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error