Identification of a binding region on Escherichia coli heat-stable enterotoxin to intestinal guanylyl cyclase C |
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Authors: | Hasegawa Makoto Kawano Yuki Matsumoto Kazuya Hidaka Yuji Sato Takashi Shimonishi Yasutsugu |
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Affiliation: | (1) Division of Protein Organic Chemistry, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, 565 Suita-shi, Osaka, Japan |
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Abstract: | Summary 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. |
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Keywords: | Photoaffinity labeling Cross-linking p-Azidophenylalanine |
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