Proteolytic degradation of human antimicrobial peptide LL-37 by Bacillus anthracis may contribute to virulence

Antimicrob Agents Chemother. 2006 Jul;50(7):2316-22. doi: 10.1128/AAC.01488-05.

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 [GI50], 1 microg/ml). B. cereus and B. thuringiensis showed intermediate levels of resistance to killing (GI50s, 33 microg/ml and 37 microg/ml, respectively). B. anthracis showed the highest level of resistance (GI50s, 40 to 66 microg/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.

MeSH terms

  • Antimicrobial Cationic Peptides / metabolism*
  • Antimicrobial Cationic Peptides / pharmacology
  • Bacillus / classification
  • Bacillus / drug effects
  • Bacillus / growth & development
  • Bacillus / physiology
  • Bacillus anthracis / drug effects
  • Bacillus anthracis / enzymology*
  • Bacillus anthracis / growth & development
  • Bacillus anthracis / pathogenicity*
  • Cathelicidins
  • Culture Media, Conditioned / pharmacology
  • Drug Resistance, Bacterial*
  • Humans
  • Metalloproteases / antagonists & inhibitors
  • Metalloproteases / metabolism*
  • Microbial Sensitivity Tests / methods
  • Protease Inhibitors / pharmacology
  • Spores, Bacterial / drug effects
  • Virulence

Substances

  • Antimicrobial Cationic Peptides
  • Cathelicidins
  • Culture Media, Conditioned
  • Protease Inhibitors
  • Metalloproteases