Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8

Biol Chem. 2006 Jul;387(7):911-5. doi: 10.1515/BC.2006.115.

Abstract

Pseudomonas aeruginosa secretes several proteases considered as important virulence factors. In this report we present data indicating that two key proinflammatory cytokines, interleukin-6 (IL-6) and IL-8, are substrates for pseudolysin (elastase) and aeruginolysin (alkaline protease). While IL-6 was totally digested by both proteases, a long form of IL-8 (IL-8-77) was first rapidly processed into a 72-residue form with enhanced chemokine activity, then very slowly degraded. Interestingly, aeruginolysin bearing two additional residues at the N-terminus (Leu-Lys-aeruginolysin) in the absence of calcium degraded both IL-6 and IL-8-72 far more efficiently than the shorter form of the enzyme.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Endopeptidases / metabolism*
  • Hydrolysis
  • Interleukin-6 / metabolism*
  • Interleukin-8 / metabolism*
  • Protein Binding
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Interleukin-6
  • Interleukin-8
  • Endopeptidases
  • alkaline protease