E. COLI HEAT STABLE ENTEROTOXIN AND INTESTINAL RECEPTOR

某些致病菌释放的热稳定肠毒素 大肠杆菌菌株与刷状缘上的糖蛋白结合 肠上皮细胞表面，激活鸟苷酸环化酶， 导致严重的水样腹泻 该肽已被证明具有 核心氨基酸序列与其它多肽释放的肽同源 细菌和真核生物。 这些E.大肠杆菌是 感染性腹泻的主要原因。 这项提案的长期目标是 为了理解配体-受体蛋白相互作用的本质， 使用生物化学和分子方法。 的具体目标 本文描述的实验将是：（1）鉴定推定的肠 与热稳定的、细菌的 肠毒素和（2）确定刷的一级结构 E.肠边缘受体大肠杆菌热稳定肠毒素 蛋白质和cDNA序列分析。

The heat stable enterotoxin released by some strains of pathogenic strains of Escherichia coli binds to a glycoprotein on the brush border surface of intestinal epithelial cells, activating guanylate cyclase and causing a severe watery diarrhea. This peptide has been shown to have core amino acid sequence homology with peptides released by other bacteria and by eukaryotic organisms. Such strains of E. Coli are a major cause of infectious diarrhea. The long goal of this proposal is to understand the nature of the ligand-receptor protein interaction by use of biochemical and molecular approaches. The specific objectives of experiments described herein will be: (1) to identify the putative gut hormone or peptide homologous to the family of heat-stable, bacterial enterotoxins and (2) to determine the primary structure of the brush border intestinal receptor of E. Coli heat stable enterotoxin by sequence analysis of protein and cDNA.