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Antimicrobial Agents and Chemotherapy, July 2006, p. 2316-2322, Vol. 50, No. 7
0066-4804/06/$08.00+0     doi:10.1128/AAC.01488-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Proteolytic Degradation of Human Antimicrobial Peptide LL-37 by Bacillus anthracis May Contribute to Virulence

Joanne E. Thwaite,* Stephen Hibbs, Richard W. Titball, and Timothy P. Atkins

Biomedical Sciences, Dstl Porton Down, Salisbury, Wiltshire SP4 0JQ, United Kingdom

Received 18 November 2005/ Returned for modification 3 February 2006/ Accepted 29 March 2006

In this paper we report on the susceptibilities of a range of Bacillus species to the human antimicrobial peptide LL-37. B. subtilis showed a low level of resistance to killing by LL-37 (50% growth-inhibitory concentration [GI50], 1 µg/ml). B. cereus and B. thuringiensis showed intermediate levels of resistance to killing (GI50s, 33 µg/ml and 37 µg/ml, respectively). B. anthracis showed the highest level of resistance (GI50s, 40 to 66 µg/ml). The degradation of LL-37 by B. anthracis culture supernatant was blocked by the metalloprotease inhibitors EDTA and 1,10-phenanthroline, and the gene encoding the protease responsible for LL-37 degradation was not plasmid borne. Our findings suggest that alongside the classical plasmid-based virulence determinants, extracellular metalloproteases of B. anthracis may play a role in survival in the host.

* Corresponding author. Mailing address: Biomedical Sciences, Dstl Porton Down, Salisbury, Wiltshire SP4 0JQ, United Kingdom. Phone: 44-1980-613262. Fax: 44-1980-614307. E-mail: jethwaite{at}dstl.gov.uk.

Antimicrobial Agents and Chemotherapy, July 2006, p. 2316-2322, Vol. 50, No. 7
0066-4804/06/$08.00+0     doi:10.1128/AAC.01488-05
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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