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J. Biol. Chem., Vol. 276, Issue 51, 48371-48375, December 21, 2001
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From the Viruses have evolved a number of strategies to
gain entry and replicate in host target cells that, for human
immunodeficiency virus (HIV) and the poxvirus, myxoma virus, involve
appropriating chemokine receptors. In this report we demonstrate that
activation of multiple intracellular tyrosine
phosphorylation events rapidly ensues following virus
adsorption to NIH 3T3.CD4.CCR5 cells and affects the ultimate level of
myxoma virus replication. UV-inactivated myxoma virus induces the rapid
phosphorylation of CCR5 on tyrosine residues, the association of CCR5
with Jaks and p56lck, and their phosphorylation-activation
within minutes of virus adsorption. Additionally, we provide evidence
for myxoma virus-inducible signal transducers and activators of
transcription (Stat) and insulin receptor substrate (IRS) activation.
In contrast to CCR5 activation effected by HIV Env protein, these
myxoma virus-inducible phosphorylation events are not sensitive to
pertussis toxin treatment. Moreover, in cells that are non-permissive
for myxoma virus infection, we provide evidence that myxoma virus fails
to invoke this tyrosine phosphorylation cascade. Consistent with the
observation that infection of CCR5-expressing cells is blocked by
herbimycin A and the Jak 2 inhibitor, tyrophostin AG490, we infer that
viral infectivity may be dependent on non-G-protein-coupled signal
transduction pathways triggered by the infecting myxoma virus particle.
This provides a novel post-binding mechanism by which viruses can
co-opt a cellular receptor to permit productive virus infection.
Poxvirus Infection Rapidly Activates Tyrosine Kinase Signal
Transduction*
§,§,
,**, and§§
Division of Cell and Molecular
Biology, Toronto General Research Institute, University Health Network,
Canadian Blood Services Building, Toronto, Ontario M5G 2M1, Canada, the
Department of Immunology, University of Toronto, Toronto,
Ontario M5S 1A8, Canada, the ¶ Section of
Hematology-Oncology, University of Illinois and West Side Veterans
Affairs Hospital, Chicago, Illinois 60607, The John P. Robarts
Research Institute and Department of Microbiology and Immunology,
University of Western Ontario,
London, Ontario 46G 2V4, Canada
*
This work was supported by Canadian Institutes of Health
Research Grants MOP-42564 (to E. N. F.) and MOP-37993
(to G. M.), by National Institutes of Health Grants CA73381 and
CA77816, and by a Merit Review grant form the Department of Veterans
Affairs (to L. C. P.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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