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A more recent version of this article appeared on February 6, 2004
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M308978200v1
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Papers In Press, published online ahead of print November 17, 2003
J. Biol. Chem, 10.1074/jbc.M308978200
Submitted on August 13, 2003
Revised on November 11, 2003
Accepted on November 17, 2003

Lck dephosphorylation at Y394 and inhibition of T cell antigen receptor signaling by Yersinia phosphatase YopH

Andres Alonso, Nunzio Bottini, Shane Bruckner, Souad Rahmouni, Scott Williams, Stephen P. Schoenberger, and Tomas Mustelin

Program of Signal Transduction, The Burnham Institute, La Jolla, CA 92037

Corresponding Author: tmustelin{at}burnham-inst.org

A key virulence factor for Yersinia pestis, the etiologic agent of plague, is the tyrosine phosphatase YopH, which the bacterium injects into host cells. We report that treatment of human T lymphocytes with a recombinant membrane-permeable YopH resulted in severe reduction in intracellular tyrosine phosphorylation and inhibition of T cell activation. The primary signal transducer for the T cell antigen receptor, the Lck tyrosine kinase, was specifically precipitated by a substrate-trapping YopH mutant and Lck was dephosphorylated at its positive regulatory site, Y394, in cells containing active YopH. By turning off Lck, YopH blocks T cell antigen receptor signaling at its very first step, effectively preventing the development of a protective immune response against this lethal bacterium.


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