Abstract
The protein encoded by herpesvirus saimiri transforming gene STP-C488 was identified and characterized. Antibodies were produced in rabbits by immunization with keyhole limpet hemocyanin-conjugated synthetic peptides specific for the predicted sequence of STP-C488. STP-C488-encoded protein was detected in recombinant Escherichia coli, transformed Rat-1 cells, transfected COS-1 cells, and in common marmoset T lymphocytes immortalized by herpesvirus saimiri strain 488. STP-C488 protein was sensitive to treatment by bacterial collagenase, consistent with the 18 uninterrupted collagenlike repeats predicted by the DNA sequence. The apparent molecular size of STP-C488 in sodium dodecyl sulfate (SDS)-polyacrylamide gels (20 to 22 kDa) was considerably larger than that predicted from the DNA sequence (9.9 kDa). Using indirect immunofluorescence tests and subcellular fractionation, STP-C488 was found to be membrane bound, primarily in perinuclear compartments. The 18 uninterrupted collagenlike repeats, sensitivity to collagenase, location in the cell, and anomalous migration through SDS-polyacrylamide gels suggest an unusual, membrane-associated, fibrous structure for this transforming herpesvirus oncoprotein.