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

Author:

Thwaite Joanne E.1,Hibbs Stephen1,Titball Richard W.1,Atkins Timothy P.1

Affiliation:

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

Abstract

ABSTRACT 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 [GI 50 ], 1 μg/ml). B. cereus and B. thuringiensis showed intermediate levels of resistance to killing (GI 50 s, 33 μg/ml and 37 μg/ml, respectively). B. anthracis showed the highest level of resistance (GI 50 s, 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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

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