Protein kinase activity associated with a cell cycle regulated, membrane-bound Epstein-Barr virus induced early antigen.
An Epstein-Barr virus protein associated with the restricted component of the early antigen complex was characterized in this study. This protein was of particular interest because of its homology to polyoma middle T antigen and to the product of the bcl-2 oncogene. The results from this study reveal that this protein had a number of unusual properties in comparison with other polypeptides associated with the early antigen complex. For example, the synthesis of this membrane-associated antigen was regulated by the cell cycle, and its expression was compatible with cell survival. Functional studies reveal that immunoprecipitates containing this protein exhibited a threonine-serine-specific protein kinase activity. The results suggest that this protein might function in both the immortalization and replication cycles of this virus.
Kocache
M M
MM
Department of Microbiology, Georgetown University Medical School, Washington, D.C. 20007.
Pearson
G R
GR
D000596:Amino Acids / Q000032:analysis; D000956:Antigens, Viral / Q000096:biosynthesis* / Q000502:physiology; D002087:Butyrates / Q000494:pharmacology; D020148:Butyric Acid; D002453:Cell Cycle / Q000187:drug effects; D002458:Cell Fractionation; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D004854:Herpesvirus 4, Human / Q000201:enzymology / Q000502:physiology*; D006801:Humans; D007158:Immunologic Techniques; D008565:Membrane Proteins / Q000378:metabolism* / Q000502:physiology; D009943:Organophosphorus Compounds / Q000032:analysis; D011494:Protein Kinases / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014779:Virus Replication / Q000187:drug effects
D000596:Amino Acids; D000956:Antigens, Viral; D002087:Butyrates; C033305:Epstein-Barr virus early antigen; D008565:Membrane Proteins; D009943:Organophosphorus Compounds; D020148:Butyric Acid; D011494:Protein Kinases; D013755:Tetradecanoylphorbol Acetate