Differentiation of thermolysins and serralysins by monoclonal antibodies.
Two monoclonal antibodies (MAbs) to a 36-kDa extracellular metalloprotease (PSCP) from Burkholderia (Pseudomonas) cepacia were found to react with thermolysin, Pseudomonas aeruginosa elastase, alkaline protease (Apr) and LasA, Serratia marcescens protease (SMP), Aeromonas hydrophila protease (AhP), and both the lethal factor (LF) and protective antigen (PA) of Bacillus anthracis on immunoblots. The MAbs were capable of neutralising the proteolytic activity of thermolysin, P. aeruginosa elastase and PSCP but not that of Apr, SMP, and AhP. These results suggest that these MAbs may be able to differentiate between the thermolysin and serralysin family of metalloproteases on the basis of their neutralisation capability and could, therefore, be useful tools in the characterisation of new bacterial proteases.
Kooi
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C
Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Alberta, Canada.
Sokol
P A
PA
D016980:Aeromonas hydrophila / Q000276:immunology; D000911:Antibodies, Monoclonal / Q000276:immunology*; D001408:Bacillus anthracis / Q000276:immunology; D016956:Burkholderia cepacia / Q000276:immunology*; D003429:Cross Reactions / Q000276:immunology; D010450:Endopeptidases / Q000276:immunology; D015151:Immunoblotting; D008055:Lipids / Q000276:immunology; D008666:Metalloendopeptidases / Q000276:immunology*; D019158:N-Acetylneuraminic Acid / Q000276:immunology; D009500:Neutralization Tests; D010196:Pancreatic Elastase / Q000276:immunology; D011550:Pseudomonas aeruginosa / Q000276:immunology; D012706:Serratia marcescens / Q000276:immunology; D013820:Thermolysin / Q000276:immunology*
D000911:Antibodies, Monoclonal; D008055:Lipids; C054080:lipid-associated sialic acid; D010450:Endopeptidases; D010196:Pancreatic Elastase; D008666:Metalloendopeptidases; D013820:Thermolysin; C095666:serralysin; D019158:N-Acetylneuraminic Acid