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. 1998 May 1;280(5364):734-7.
doi: 10.1126/science.280.5364.734.

Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor

N S Duesbery  1 , C P Webb, S H Leppla, V M Gordon, K R Klimpel, T D Copeland, N G Ahn, M K Oskarsson, K Fukasawa, K D Paull, G F Vande Woude
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Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor

N S Duesbery et al. Science. .

Abstract

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.

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Comment in

  • New clue to how anthrax kills.
    Strauss E. Strauss E. Science. 1998 May 1;280(5364):676. doi: 10.1126/science.280.5364.676. Science. 1998. PMID: 9599144 No abstract available.
  • How anthrax kills.
    Hanna P. Hanna P. Science. 1998 Jun 12;280(5370):1671, 1673-4. doi: 10.1126/science.280.5370.1671c. Science. 1998. PMID: 9660700 No abstract available.

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