1995
DOI: 10.1016/0014-5793(95)00267-d
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Characterization of a highly toxic, large molecular size heat‐stable enterotoxin produced by a clinical isolate of Yersinia enterocolitica

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Cited by 17 publications
(8 citation statements)
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“…In contrast to YSTa and YSTb, the mature form of YSTc was very long (53 AA), representing the largest molecular size toxin in the family of currently known STs. This secreted peptide was composed of the pro-and mature domain of the polypeptide (Yoshino et al, 1995b). The presence of the pro-domain in the secreted mature toxin suggests that in Y. enterocolitica, the proteolytic processing of the prodomain is not essential for the secretion of YSTc to the extracellular compartment through the outer membrane.…”
Section: Superantigens Of Y Pseudotuberculosismentioning
confidence: 96%
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“…In contrast to YSTa and YSTb, the mature form of YSTc was very long (53 AA), representing the largest molecular size toxin in the family of currently known STs. This secreted peptide was composed of the pro-and mature domain of the polypeptide (Yoshino et al, 1995b). The presence of the pro-domain in the secreted mature toxin suggests that in Y. enterocolitica, the proteolytic processing of the prodomain is not essential for the secretion of YSTc to the extracellular compartment through the outer membrane.…”
Section: Superantigens Of Y Pseudotuberculosismentioning
confidence: 96%
“…In contrast to YSTa, YSTb is produced in cells grown at 37°C (Yoshino et al, 1995b). YSTc was found to have an enterotoxigenic activity four times superior to those of YSTb and STh of E. coli, which had been known as the most potent STs.…”
Section: Superantigens Of Y Pseudotuberculosismentioning
confidence: 96%
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