PMID: 8985388Jan 1, 1997Paper

Tyrosine phosphorylation events during coxsackievirus B3 replication

Journal of Virology
M HuberR Kandolf

Abstract

In order to study cellular and viral determinants of pathogenicity, interactions between coxsackievirus B3 (CVB3) replication and cellular protein tyrosine phosphorylation were investigated. During CVB3 infection of HeLa cells, distinct proteins become phosphorylated on tyrosine residues, as detected by the use of antiphosphotyrosine Western blotting. Two proteins of 48 and 200 kDa showed enhanced tyrosine phosphorylation 4 to 5 h postinfection (p.i.), although virus-induced inhibition of cellular protein synthesis had already occurred 3 to 4 h p.i. Subcellular fractionation experiments revealed distinct localization of tyrosine-phosphorylated proteins of 48 and 200 kDa in the cytosol and membrane fractions of infected cells, respectively. In addition, in Vero cells infected with CVB3, echovirus (EV)11, or EV12, increased tyrosine phosphorylation of a 200-kDa protein was detected 6 h p.i. Herbimycin A, a specific inhibitor of Src-like protein tyrosine kinases, was shown to inhibit virus-induced tyrosine phosphorylations and to reduce the production of progeny virions. In contrast, in cells treated with the inhibitors staurosporine and calphostin C, the synthesis of progeny virions was not affected. Immunoprecipitation experimen...Continue Reading

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Citations

Nov 28, 2007·Annual Review of Pathology·Mitra Esfandiarei, Bruce M McManus
Dec 24, 1997·Clinical and Experimental Pharmacology & Physiology·C M CarthyB M McManus
Apr 14, 2015·Future Microbiology·Farshid S GarmaroudiBruce M McManus

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