Premium
Essential structure for full enterotoxigenic activity of heat‐stable enterotoxin produced by enterotoxigenic Escherichia coli
Author(s) -
Yoshimura Shoko,
Ikemura Haruo,
Watanabe Hiroyuki,
Aimoto Saburo,
Shimonishi Yasutsugu,
Hara Saburo,
Takeda Tae,
Miwatani Toshio,
Takeda Yoshifumi
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81129-7
Subject(s) - enterotoxigenic escherichia coli , heat stable enterotoxin , enterotoxin , residue (chemistry) , escherichia coli , disulfide bond , chemistry , amino acid residue , peptide sequence , biochemistry , amino acid , microbiology and biotechnology , biology , gene
Several analogues of heat‐stable enterotoxins (ST h and ST P ) produced by enterotoxigenic Escherichia coli were synthesized. Peptides (ST h [6–18] and ST P [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 ST h and ST P , 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.