Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8751398 | Virology | 2018 | 7 Pages |
Abstract
The papillomavirus (PV) E2 protein activates transcription and replication by recruiting cellular proteins and the E1 DNA helicase to their binding sites in the viral genome. We recently demonstrated that phosphorylation of tyrosine 102 in the bovine papillomavirus (BPV-1) E2 protein restricts these activities and that fibroblast growth factor receptor-3 (FGFR3) tyrosine kinase binds PV E2. Expression of FGFR3 decreased viral replication with both wild-type and the phenylalanine substitution at position 102, inferring that another kinase targets Y102. Here we tested FGFR- 1, â2 and â4 for association with PV E2 proteins. FGFR2 but not FGFR1 or FGFR4 co-immunoprecipitated with BPV-1 E2. We found that FGFR2 suppressed replication but did not depend on phosphorylation of BPV-1 Y102. HPV-16 and â31 E2 interacted with FGFR1, â2, and â4. These results imply that the expression and activity of FGF receptors in epithelial cells can regulate the function of E2 in viral replication.
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Authors
Marsha DeSmet, Sriramana Kanginakudru, Leny Jose, Fang Xie, Timra Gilson, Elliot J. Androphy,