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Research Letter
November 2014

Binding of the Trichodysplasia Spinulosa–Associated Polyomavirus Small T Antigen to Protein Phosphatase 2A: Elucidation of a Potential Pathogenic Mechanism in a Rare Skin Disease

Author Affiliations
  • 1Department of Dermatology, University of Texas Medical School at Houston, Houston
  • 2medical student at Baylor College of Medicine, Houston, Texas
JAMA Dermatol. 2014;150(11):1234-1236. doi:10.1001/jamadermatol.2014.1095

Trichodysplasia spinulosa is a disfiguring skin disease caused by the trichodysplasia spinulosa–associated polyomavirus (TSPyV).1 Like other polyomaviruses, TSPyV expresses the large T and small T (sT) antigens, but how these proteins regulate trichodysplasia spinulosa pathogenesis is unknown. In the closely related human pathogen Merkel cell polyomavirus, sT acts as a transforming oncoprotein in vitro because it alone is sufficient to transform rodent fibroblast cells.2 Interestingly, this mechanism does not seem to involve protein phosphatase 2A (PP2A), which is a characteristic target of other polyomaviruses’ sT antigens. Because PP2A regulates important cellular pathways, the inactivation is one of the critical steps in the polyomavirus pathomechanism. The primary purpose of this study was to determine whether TSPyV sT antigen was capable of binding PP2A; if positive, this finding would implicate specific pathways in trichodysplasia spinulosa pathogenesis.

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