Interaction of a novel form of Pseudomonas aeruginosa alkaline protease (aeruginolysin) with interleukin-6 and interleukin-8.
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.
Matheson
Nancy R
NR
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA.
Potempa
Jan
J
Travis
James
J
D001426:Bacterial Proteins / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D015850:Interleukin-6 / Q000378:metabolism*; D016209:Interleukin-8 / Q000378:metabolism*; D011485:Protein Binding; D013379:Substrate Specificity
D001426:Bacterial Proteins; D015850:Interleukin-6; D016209:Interleukin-8; D010450:Endopeptidases; C087822:alkaline protease