Enteroaggregative Escherichia coli strains secrete a heat-labile toxin antigenically related to E. coli hemolysin.
A protein toxin of approximately 120,000 Da secreted by nonhemolytic enteroaggregative Escherichia coli strains cross-reacted in Western blots (immunoblots) with antibodies raised against the C-terminal region of E. coli hemolysin. Treatment of HEp-2 cells with enteroaggregative E. coli or culture supernatants caused elevation of intracellular calcium and stimulated calcium-dependent protein phosphorylation.
Baldwin
T J
TJ
Department of Genetics, University of Leicester, United Kingdom.
Knutton
S
S
Sellers
L
L
Hernandez
H A
HA
Aitken
A
A
Williams
P H
PH
D000942:Antigens, Bacterial / Q000276:immunology*; D001427:Bacterial Toxins / Q000276:immunology*; D002118:Calcium / Q000378:metabolism; D003967:Diarrhea / Q000209:etiology; D004768:Enterotoxins / Q000276:immunology*; D004926:Escherichia coli / Q000378:metabolism* / Q000472:pathogenicity; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins / Q000276:immunology*; D006801:Humans; D010766:Phosphorylation; D011506:Proteins / Q000378:metabolism
D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D006460:Hemolysin Proteins; D011506:Proteins; C027538:heat-labile enterotoxin, E coli; D002118:Calcium