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Herpesvirus saimiri protein StpB associates with cellular Src
Simon Hör1, Armin Ensser1, Christine Reiss1
1Institut für Klinische und Molekulare Virologie, Universität Erlangen-Nürnberg, Schloßgarten 4, D-91054 Erlangen, Germany1.
The Journal of General Virology
|February 13, 2001
Summary
Herpesvirus saimiri subgroup B shows lower T lymphocyte transformation efficiency. This is despite its StpB protein binding to c-Src, suggesting other factors influence transformation.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Herpesvirus saimiri (HVS) is a T-lymphotropic virus.
- HVS isolates are classified into subgroups A, B, and C.
- Subgroup B HVS isolates exhibit reduced T lymphocyte transformation efficiency compared to subgroups A and C.
Purpose of the Study:
- To investigate the molecular mechanisms underlying the differential T lymphocyte transformation efficiency of HVS subgroups.
- To characterize the HVS saimiri transforming protein (Stp) homolog in subgroup B.
Main Methods:
- Sequence analysis of HVS subgroup B strain SMHI.
- Identification and characterization of the StpB protein.
- Analysis of StpB interaction with cellular Src kinase domains.
Main Results:
- Subgroup B strain SMHI encodes a novel protein, StpB, analogous to StpA and StpC.
- StpB shares limited sequence similarity with StpA and StpC.
- StpB interacts with the SH2 domain of cellular Src, similar to StpA.
Conclusions:
- The lower T lymphocyte transformation efficiency of HVS subgroup B is not solely determined by c-Src binding.
- Additional viral or cellular factors likely regulate the transforming capacity of HVS subgroup B strains.