Nicking sites in a subunit of cholera toxin and Escherichia coli heat-labile enterotoxin for Vibrio cholerae hemagglutinin/protease.
We analyzed the nicking site of the A subunit of Escherichia coli heat-labile enterotoxin for hemagglutinin/protease produced by Vibrio cholerae non-O1 (NAG-HA/P). The determined nicking site was the Thr193-Ile194 junction, which was distinct from that for a protease of V. cholerae (Ichinose et al., European Journal of Epidemiology 8, 743-747, 1992). We further analyzed proteolytic cleavage by NAG-HA/P of a synthetic peptide corresponding to the nicking region of cholera toxin A subunit and determined the cleavage site to be preferentially between Ser194 and Met195, and in addition between Ser193 and Ser194.
Department of Bacterial Infections, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
A
A
Naka
T
T
Iida
T
T
Ohara
K
K
Yamamoto
T
T
Miwatani
T
T
Honda
D001427:Bacterial Toxins / Q000378:metabolism*; D004768:Enterotoxins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins; D006388:Hemagglutinins / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000378:metabolism*; D014734:Vibrio cholerae / Q000201:enzymology*
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D006388:Hemagglutinins; C037420:stN protein, Vibrio cholerae; C027538:heat-labile enterotoxin, E coli; D008666:Metalloendopeptidases; C039814:hemagglutinin-protease