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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Phosphorylation of cytokeratin 17 by herpes simplex virus type 2 US3 protein kinase.

We previously reported the establishment of an HEp2 cell line which expresses the US3 protein kinase (PK) of herpes simplex virus type 2 (HSV-2) upon induction with IPTG. Here we report that expression, phosphorylation and ubiquitination of cytokeratin 17 (CK17) are enhanced in US3-expressing HEp2 cells. In vitro kinase and co-immunoprecipitation assays provided evidence that US3 PK directly phosphorylates CK17. Expression of US3 PK caused a significant decrease in filamentous staining of CK17, suggesting that phosphorylation of CK17 by US3 PK causes a disruption of intermediate filaments. Our observations suggest a role for US3 in the regulation of CKs and intermediate filaments in cells. Moreover, we found that infection of a keratinocyte-derived cell line, A431, with a US3-deficient virus, results in cytopathic effects that are morphologically distinct from those induced by wild-type and revertant viruses, suggesting that US3 PK may be important for interaction between HSV-2 and peripheral epithelial cells.[1]


  1. Phosphorylation of cytokeratin 17 by herpes simplex virus type 2 US3 protein kinase. Murata, T., Goshima, F., Nishizawa, Y., Daikoku, T., Takakuwa, H., Ohtsuka, K., Yoshikawa, T., Nishiyama, Y. Microbiol. Immunol. (2002) [Pubmed]
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