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The Journal of Medical Microbiology, Vol 45, Issue 3 219-225, Copyright © 1996 by Society for General Microbiology

JOURNAL ARTICLE

Differentiation of thermolysins and serralysins by monoclonal antibodies

C. Kooi and P. A. Sokol
Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Alberta, Canada.

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.




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