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.
Naka
A
A
Department of Bacterial Infections, Research Institute for Microbial Diseases, Osaka University, Suita, Japan.
Iida
T
T
Ohara
T
T
Yamamoto
K
K
Miwatani
T
T
Honda
T
T
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