E. COLI HEAT STABLE ENTEROTOXIN AND INTESTINAL RECEPTOR

几株致病菌所释放的耐热肠毒素 大肠杆菌菌株与灌木丛边缘的一种糖蛋白结合 肠上皮细胞表面，激活鸟苷环化酶和 导致严重的水样腹泻。这种多肽已被证明具有 核心氨基酸序列与其他生物释放的多肽的同源性 细菌和真核生物。这些大肠杆菌菌株是一种 感染性腹泻的主要原因。这项提议的长期目标是 通过以下方法了解配体-受体蛋白相互作用的性质 使用生化和分子方法。的具体目标 这里描述的实验将是：(1)识别假定的内脏 与耐热细菌家族同源的激素或多肽 肠毒素和(2)确定刷子的一级结构 大肠埃希氏菌耐热肠毒素的边界肠道受体 蛋白质和cDNA的序列分析。

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.