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Science 1 May 1998:
Vol. 280. no. 5364, pp. 734 - 737
DOI: 10.1126/science.280.5364.734
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Reports

Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor

Nicholas S. Duesbery, Craig P. Webb, Stephen H. Leppla, Valery M. Gordon, Kurt R. Klimpel, * Terry D. Copeland, Natalie G. Ahn, Marianne K. Oskarsson, Kenji Fukasawa, Ken D. Paull, George F. Vande Woude dagger

Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin, lethal factor (LF), is suspected to be a metalloprotease, but no physiological substrates have been identified. Here it is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 (MAPKK1 and MAPKK2) and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway. The identification of a cleavage site for LF may facilitate the development of LF inhibitors.

N. S. Duesbery, C. P. Webb, T. D. Copeland, M. K. Oskarsson, G. F. Vande Woude, Advanced BioScience Laboratories-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, Post Office Box B, Frederick, MD 21702, USA.
S. H. Leppla, V. M. Gordon, K. R. Klimpel, National Institute of Dental Research-National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA.
N. G. Ahn, Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Campus Box 215, Boulder, CO 80309, USA.
K. Fukasawa, Department of Cell Biology, University of Cincinnati, College of Medicine, P.O. Box 670521, Cincinnati, OH 45267, USA.
K. D. Paull, Division of Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
*   Present address: Biopraxis, Post Office Box 9100-78, San Diego, CA 92191, USA.

dagger    To whom correspondence should be addressed.

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M. Moayeri, J. I. Webster, J. F. Wiggins, S. H. Leppla, and E. M. Sternberg (2005)
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J. Immunol. 174, 4934-4941
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J. Immunol. 174, 4966-4971
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R. G. Panchal, K. M. Halverson, W. Ribot, D. Lane, T. Kenny, T. G. Abshire, J. W. Ezzell, T. A. Hoover, B. Powell, S. Little, et al. (2005)
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J. Biol. Chem. 279, 23349-23356
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J. Biol. Chem. 279, 20563-20566
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Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: An anthrax toxin receptor.
D. B. Lacy, D. J. Wigelsworth, H. M. Scobie, J. A. T. Young, and R. J. Collier (2004)
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X. Cui, M. Moayeri, Y. Li, X. Li, M. Haley, Y. Fitz, R. Correa-Araujo, S. M. Banks, S. H. Leppla, and P. Q. Eichacker (2004)
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Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection.
Y. Shen, N. L. Zhukovskaya, M. I. Zimmer, S. Soelaiman, P. Bergson, C.-R. Wang, C. S. Gibbs, and W.-J. Tang (2004)
PNAS 101, 3242-3247
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Exogenous Gamma and Alpha/Beta Interferon Rescues Human Macrophages from Cell Death Induced by Bacillus anthracis.
J. A. Gold, Y. Hoshino, S. Hoshino, M. B. Jones, A. Nolan, and M. D. Weiden (2004)
Infect. Immun. 72, 1291-1297
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Cutting Edge: Anthrax Lethal Toxin Inhibits Activation of IFN-Regulatory Factor 3 by Lipopolysaccharide.
O. Dang, L. Navarro, K. Anderson, and M. David (2004)
J. Immunol. 172, 747-751
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Anthrax Lethal Toxin Induces Human Endothelial Cell Apoptosis.
J. E. Kirby (2004)
Infect. Immun. 72, 430-439
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Binding of Anthrax Toxin to Its Receptor Is Similar to {alpha} Integrin-Ligand Interactions.
K. A. Bradley, J. Mogridge, G. Jonah, A. Rainey, S. Batt