Essential structure for full enterotoxigenic activity of heat‐stable enterotoxin produced by enterotoxigenic Escherichia coli

FEBS Letters

Takeda, Tae¹  Watanabe, Hiroyuki³  Ikemura, Haruo³  Aimoto, Saburo³  Hara, Saburo²  Shimonishi, Yasutsugu³  Yoshimura, Shoko³  Takeda, Yoshifumi⁴  Miwatani, Toshio¹ 

[1] Institute for Microbial Diseases, Osaka University, Suita, Osaka 565 Japan;Department of Chemistry, College of Science, Osaka University, Toyonaka, Osaka 560 Japan;Institute for Protein Research, Osaka University, Suita, Osaka 565 Japan;The Institute of Medical Science, The University of Tokyo, Minato-ku, Tokyo 108, Japan

关键词: Enterotoxigenic E. coli;    Heat-stable enterotoxin;    Structure;    Synthesis;   

DOI  :  10.1016/0014-5793(85)81129-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown