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J. Biol. Chem., Vol. 279, Issue 6, 4922-4928, February 6, 2004
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¶
From the
Program of Signal Transduction, Cancer Research Center, The Burnham Institute, La Jolla, California 92037 and La Jolla Institute for Allergy and Immunology, San Diego, California 92121
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, Tyr-394, 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.
Received for publication, August 13, 2003 , and in revised form, November 11, 2003.
* This work was supported by a fellowship from the American-Italian Cancer Foundation and Grant AI53114 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ To whom correspondence should be addressed: Program of Signal Transduction, The Burnham Inst., 10901 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-713-6270; Fax: 858-713-6274; E-mail: tmustelin{at}burnham-inst.org.
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