Pathogenesis of serratial infection: activation of the Hageman factor-prekallikrein cascade by serratial protease.
A serratial protease with an apparent molecular weight of 56,000 (56K protease), which had been purified from the culture supernatant of a strain of Serratia marcescens isolated from a corneal lesion of a human eye [Matsumoto, K. et al. (1984) J. Bacteriol. 157, 225-232], greatly enhanced vascular permeability when injected into guinea pig skin. The 56K protease, which requires zinc ion for activity, was found to possess plasma kallikrein-like properties in vitro as judged by (i) preferential amidolysis of carbobenzoxy-Phe-Arg-4-methylcoumaryl-7-amide and Pro-Phe-Arg-4-methylcoumaryl-7-amide, which are known substrates for plasma kallikrein; (ii) release of kinin from high-molecular-weight kininogen; and (iii) prompt activation of Hageman factor followed by generation of kallikrein from plasma prekallikrein. These results suggest that the 56K protease enhances vascular permeability through activation of a Hageman factor-kallikrein-kinin pathway in vivo, and this molecular process appears to be a rational mechanism of enhancement of permeability and serratial pathogenesis.
D000818:Animals; D001424:Bacterial Infections / Q000503:physiopathology*; D001777:Blood Coagulation; D003316:Corneal Diseases / Q000382:microbiology* / Q000503:physiopathology; D004789:Enzyme Activation; D005174:Factor XII / Q000378:metabolism*; D005260:Female; D006168:Guinea Pigs; D006801:Humans; D005779:Immunodiffusion; D007610:Kallikreins / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011288:Prekallikrein / Q000378:metabolism*; D012706:Serratia marcescens / Q000201:enzymology* / Q000472:pathogenicity; D013379:Substrate Specificity
D005174:Factor XII; D011288:Prekallikrein; D010447:Peptide Hydrolases; D007610:Kallikreins