Previous Article | Next Article ![]()
J. Virol., 01 1997, 595-600, Vol 71, No. 1
M Huber, HC Selinka and R Kandolf
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 experiments suggested that the
tyrosine-phosphorylated 200-kDa protein in CVB3-infected cells is of
cellular origin. In summary, these investigations have begun to unravel the
effect of CVB3 as well as EV11 and EV12 replication on cellular tyrosine
phosphorylation and support the importance of tyrosine phosphorylation
events for effective virus replication. Such cellular phosphorylation
events triggered in the course of enterovirus infection may enhance virus
replication.
Copyright © 1997, American Society for Microbiology
Tyrosine phosphorylation events during coxsackievirus B3 replication
Institute for Pathology, Department of Molecular Pathology, University of Tubingen, Germany.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»