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Journal of General Virology (2001), 82, 339-344.
© 2001 Society for General Microbiology

Animal: DNA Viruses

Herpesvirus saimiri protein StpB associates with cellular Src

Simon Hör1, Armin Ensser1, Christine Reiss1, Kurt Ballmer-Hofer2 and Brigitte Biesinger1

Institut für Klinische und Molekulare Virologie, Universität Erlangen-Nürnberg, Schloßgarten 4, D-91054 Erlangen, Germany1
Institute for Radiobiology at the Paul Scherrer Institute, CH-5232 Villigen-PSI, Switzerland2

Author for correspondence: Brigitte Biesinger. Present address: Department of Molecular Biology, Max-Planck-Institute for Biochemistry, Am Klopferspitz 18A, D-82152 Martinsried, Germany. Fax +49 89 8578 2454. e-mail biesing{at}biochem.mpg.de

Subgroup B isolates of Herpesvirus saimiri are less efficient in T lymphocyte transformation when compared with subgroups A or C. Here it is shown that subgroup B strain SMHI encodes a protein, StpB, at a position equivalent to those of the ORFs for the saimiri transforming proteins (Stp) of subgroups A and C. StpB shares little similarity with StpA or StpC, but interacts with the SH2 domain of cellular Src, as does StpA. Thus, factors other than c-Src binding determine the efficiency of primary T cell transformation by Herpesvirus saimiri.




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