Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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COS Cells
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Herpesvirus 2, Saimiriine* / chemistry
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Herpesvirus 2, Saimiriine* / genetics
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Herpesvirus 2, Saimiriine* / metabolism
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Intracellular Signaling Peptides and Proteins
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Molecular Sequence Data
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Open Reading Frames
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Phosphorylation
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Protein Binding
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Proto-Oncogene Proteins pp60(c-src) / chemistry
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Proto-Oncogene Proteins pp60(c-src) / metabolism*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Transfection
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Viral Proteins / chemistry
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Viral Proteins / genetics
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Viral Proteins / metabolism*
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src Homology Domains
Substances
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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Recombinant Fusion Proteins
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StpB protein, herpesvirus saimiri
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Viral Proteins
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Proto-Oncogene Proteins pp60(c-src)