• Media type: E-Article
  • Title: Proteolytic Degradation of Human Antimicrobial Peptide LL-37 by Bacillus anthracis May Contribute to Virulence
  • Contributor: Thwaite, Joanne E.; Hibbs, Stephen; Titball, Richard W.; Atkins, Timothy P.
  • imprint: American Society for Microbiology, 2006
  • Published in: Antimicrobial Agents and Chemotherapy
  • Language: English
  • DOI: 10.1128/aac.01488-05
  • ISSN: 1098-6596; 0066-4804
  • Keywords: Infectious Diseases ; Pharmacology (medical) ; Pharmacology
  • Origination:
  • Footnote:
  • Description: <jats:title>ABSTRACT</jats:title> <jats:p> In this paper we report on the susceptibilities of a range of <jats:italic>Bacillus</jats:italic> species to the human antimicrobial peptide LL-37. <jats:italic>B. subtilis</jats:italic> showed a low level of resistance to killing by LL-37 (50% growth-inhibitory concentration [GI <jats:sub>50</jats:sub> ], 1 μg/ml). <jats:italic>B. cereus</jats:italic> and <jats:italic>B. thuringiensis</jats:italic> showed intermediate levels of resistance to killing (GI <jats:sub>50</jats:sub> s, 33 μg/ml and 37 μg/ml, respectively). <jats:italic>B. anthracis</jats:italic> showed the highest level of resistance (GI <jats:sub>50</jats:sub> s, 40 to 66 μg/ml). The degradation of LL-37 by <jats:italic>B. anthracis</jats:italic> 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 <jats:italic>B. anthracis</jats:italic> may play a role in survival in the host. </jats:p>
  • Access State: Open Access