Identification and characterization of the herpesvirus saimiri oncoprotein STP-C488

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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.

Original languageEnglish (US)
Pages (from-to)6953-6960
Number of pages8
JournalJournal of Virology
Volume65
Issue number12
StatePublished - 1991
Externally publishedYes

Fingerprint

Saimiriine herpesvirus 2
Saimiriine Herpesvirus 2
Oncogene Proteins
collagenase
sodium dodecyl sulfate
Collagenases
polyacrylamide
Sodium Dodecyl Sulfate
gels
nucleotide sequences
Callithrix
Callithrix jacchus
Proteins
Membranes
proteins
synthetic peptides
Herpesviridae
COS Cells
cells
Indirect Fluorescent Antibody Technique

ASJC Scopus subject areas

  • Immunology

Cite this

Identification and characterization of the herpesvirus saimiri oncoprotein STP-C488. / Jung, J. U.; Desrosiers, Ronald Charles.

In: Journal of Virology, Vol. 65, No. 12, 1991, p. 6953-6960.

Research output: Contribution to journalArticle

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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.",
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