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Science 17 September 1999:
Vol. 285. no. 5435, pp. 1920 - 1923
DOI: 10.1126/science.285.5435.1920
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Reports

Inhibition of the Mitogen-Activated Protein Kinase Kinase Superfamily by a Yersinia Effector

Kim Orth, 1 Lance E. Palmer, 2* Zhao Qin Bao, 1 Scott Stewart, 1 Amy E. Rudolph, 1dagger James B. Bliska, 23 Jack E. Dixon 1ddagger

The bacterial pathogen Yersinia uses a type III secretion system to inject several virulence factors into target cells. One of the Yersinia virulence factors, YopJ, was shown to bind directly to the superfamily of MAPK (mitogen-activated protein kinase) kinases (MKKs) blocking both phosphorylation and subsequent activation of the MKKs. These results explain the diverse activities of YopJ in inhibiting the extracellular signal-regulated kinase, c-Jun amino-terminal kinase, p38, and nuclear factor kappa B signaling pathways, preventing cytokine synthesis and promoting apoptosis. YopJ-related proteins that are found in a number of bacterial pathogens of animals and plants may function to block MKKs so that host signaling responses can be modulated upon infection.

1 Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606, USA.
2 Department of Molecular Genetics and Microbiology,
3 Center for Infectious Diseases, School of Medicine, State University of New York at Stony Brook, Stony Brook, NY 11794-5222, USA.
*   Present address: Howard Hughes Medical Institute and Department of Immunology, University of Washington, Seattle, WA 98195, USA.

dagger    Present address: Monsanto/Searle, 800 North Lindbergh Boulevard, St. Louis, MO 631667, USA.

ddagger    To whom correspondence should be addressed. E-mail: jedixon{at}umich.edu

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PNAS 97, 9431-9436
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A role for IL-1alpha in inducing pathologic inflammation during bacterial infection.
P. H. Dube, P. A. Revell, D. D. Chaplin, R. G. Lorenz, and V. L. Miller (2001)
PNAS 98, 10880-10885
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Science. ISSN 0036-8075 (print), 1095-9203 (online)