U. Wagner et al., DEVELOPMENT AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES SPECIFIC FOR 2 DIFFERENT EXOPROTEASES OF AEROMONAS-SALMONICIDA, Journal of fish diseases, 20(3), 1997, pp. 223-235
Monoclonal antibodies (mabs) against native epitopes of Aeromonas salm
onicida strain F216.1/ 83-secreted proteases were isolated by means of
a Protease-Capture-Assay. Ten antibodies reacted with the 70-kDa seri
ne protease as judged from the molecular mass and enzymatic behaviour
of the recognized antigen. Eight other mabs bound gelatinolytic antige
ns which lacked caseinolytic properties and possessed some characteris
tics of a zinc-dependent metalloprotease. The molecular mass of these
mab-defined, immunologically crossreactive antigens were estimated to
be predominantly 108, 30 and 57 kDa. By comparing the antigen recognit
ion and epitope mapping profiles among anti-serine protease- and anti-
metalloprotease-mabs, at least six and five different epitope specific
ities were demonstrated, respectively. Both panels of mabs were shown
to recognize the two types of exoproteases in culture filtrates of str
ain MT004 and of several other typical A. salmonicida strains.