Essential Structure for Full Enterotoxigenic Activity of Heat-stable Enterotoxin Produced by Enterotoxigenic Escherichia Coli

Overview

Journal FEBS Lett

Specialty Biochemistry

Date 1985 Feb 11

PMID 3972100

Citations 28

Authors

S Yoshimura

H Ikemura

H Watanabe

S Aimoto

Y Shimonishi

S Hara

T Takeda

T MIWATANI

Y Takeda

Affiliations

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Abstract

Several analogues of heat-stable enterotoxins (STh and STp) produced by enterotoxigenic Escherichia coli were synthesized. Peptides (STh[6-18] and STp[5-17]) consisting of 13 amino acid residues from the Cys residue near the N-terminus to the Cys residue near the C-terminus and linked by three disulfide bonds had the same biological and immunological properties as native STh and STp, respectively. The results indicated that the sequence with the 13 amino acid residues and three disulfide linkages is essential for full biological activity of ST.

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