USE OF MONOCLONAL-ANTIBODIES TO IDENTIFY PHOSPHOLIPASE-C AS THE ENTEROTOXIC FACTOR OF THE BIFUNCTIONAL HEMOLYSIN-PHOSPHOLIPASE-C MOLECULE OF VIBRIO-CHOLERAE-O139
S. Pal et al., USE OF MONOCLONAL-ANTIBODIES TO IDENTIFY PHOSPHOLIPASE-C AS THE ENTEROTOXIC FACTOR OF THE BIFUNCTIONAL HEMOLYSIN-PHOSPHOLIPASE-C MOLECULE OF VIBRIO-CHOLERAE-O139, Infection and immunity, 66(8), 1998, pp. 3974-3977
Two hybrid clones producing monoclonal antibodies (MAbs) raised agains
t the purified enterotoxic hemolysin-phospholipase C (HlyPC) bifunctio
nal molecule of a Vibrio cholerae O139 strain were used to study its e
nterotoxicity in relation to its hemolytic and enzymatic activities. F
ab fragments of MAbs from ascites produced by the two hybrids neutrali
zed the hemolytic activity of HlyPC, leaving the enzymatic activity un
affected. In ligated rabbit ileal loop and infant mouse intestine, the
Fab fragments of the MAbs were not able to neutralize the enterotoxic
ity of HlyPC, suggesting that PC rather than Hly is the enterotoxic mo
iety of the molecule, The enterotoxicity of the purified PC molecule i
solated from an Hly(-) spontaneous mutant of the HlyPC-producing paren
t strain further confirms this contention, The Hly molecule isolated f
rom a PC-mutant was not diarrheagenic.