Letters in Peptide Science

, Volume 4, Issue 1, pp 1–11 | Cite as

Identification of a binding region onEscherichia coli heat-stable enterotoxin to intestinal guanylyl cyclase C

  • Makoto Hasegawa
  • Yuki Kawano
  • Kazuya Matsumoto
  • Yuji Hidaka
  • Takashi Sato
  • Yasutsugu Shimonishi


The heat-stable enterotoxin (ST), produced byEscherichia coli, causes acute diarrhea in infants and domestic animals by activation of the intestinal membrane-bound receptor, guanylyl cyclase C. We have investigated a region on the ST molecule, which is recognized by the receptor, by introducing a photochromophore,p-azidophenylalanine (Pap), into three different regions of STp(4–17), which has the full toxic activity. Each ST analog bound to the receptor, but only STp(4–17) containing a Pap residue at position 11 in the central portion of the ST molecule, showed a high efficiency in the reaction which cross-linked with the receptor by UV radiation. These data clearly demonstrate that the region of the ST molecule encompassing the Asn11 residue directly interacts with the receptor.


Photoaffinity labeling Cross-linking p-Azidophenylalanine 



heat-stable enterotoxin produced by enterotoxigenicEscherichia coli

E. coli

Escherichia coli


ST elaborated by a strain of enterotoxigenicE. coli isolated from pig


guanylyl cyclase C






reversed-phase high-performance liquid chromatography


sodium dodecyl sulfate polyacrylamide gel electrophoresis


circular dichroism


enzyme-linked immunosorbent assay


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Copyright information

© ESCOM Science Publishers 1997

Authors and Affiliations

  • Makoto Hasegawa
    • 1
  • Yuki Kawano
    • 1
  • Kazuya Matsumoto
    • 1
  • Yuji Hidaka
    • 1
  • Takashi Sato
    • 1
  • Yasutsugu Shimonishi
    • 1
  1. 1.Division of Protein Organic Chemistry, Institute for Protein ResearchOsaka UniversitySuita-shi, OsakaJapan

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