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Infection and Immunity, January 2004, p. 219-228, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.219-228.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Camelysin Is a Novel Surface Metalloproteinase from Bacillus cereus

Gregor Grass,1 Angelika Schierhorn,2 Eduard Sorkau,3 Helmut Müller,3 Peter Rücknagel,4 Dietrich H. Nies,1 and Beate Fricke5*

Institute for Microbiology,1 Institute of Biochemistry, Faculty of Life Sciences,2 Institute for Analytical and Environmental Chemistry, Department of Chemistry, Martin Luther University,3 Max Planck Institute for Protein Folding, D-06120 Halle,4 Institute of Biochemistry, Medical Faculty, Martin Luther University, D-06097 Halle, Germany5

Received 14 July 2003/ Returned for modification 2 September 2003/ Accepted 10 October 2003

Bacillus cereus frequently causes food poisoning or nosocomial diseases. Vegetative cells express the novel surface metalloproteinase camelysin (casein-cleaving metalloproteinase) during exponential growth on complex, peptide-rich media. Camelysin is strongly bound to the cell surface and can be solubilized only by detergents or butanol. Camelysin spontaneously migrates from the surface of intact bacterial cells to preformed liposomes. The complete sequence of the camelysin-encoding gene, calY, was determined by reverse PCR on the basis of the N-terminal sequence and some internal tryptic cleavage peptides. The calY gene codes for a polypeptide of 21.569 kDa with a putative signal peptide of 27 amino acids (2.513 kDa) preceding the mature protein (19.056 kDa). Although the predicted amino acid sequence of CalY does not exhibit a typical metalloprotease consensus sequence, high-pressure liquid chromatography-purified camelysin contains one zinc ion per protein molecule. Matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and tryptic peptide mass fingerprinting confirmed the identity of this zinc-binding protein as CalY. Disruption of the calY gene results in a strong decrease in the cell-bound proteolytic activity on various substrates.

* Corresponding author. Mailing address: Institute for Physiological Chemistry, Medical Faculty, Martin Luther University, 06097 Halle, Germany. Phone: 49/0345/5573838. Fax: 49/0345/5573811. E-mail: beate.fricke{at}medizin.uni-halle.de.

Editor: F. C. Fang

Infection and Immunity, January 2004, p. 219-228, Vol. 72, No. 1
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.1.219-228.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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