STUDIES OF THE STRUCTURE AND FUNCTION OF PERTUSSIS TOXIN

百日咳毒素的结构和功能研究

• 批准号: 3748118
• 负责人: D L BURNS
• 金额: --
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3748118
• 关键词: Bordetella pertussis; cell membrane; chemical binding; chemical structure function; glycosphingolipids; membrane proteins; mutant; oligosaccharides; pertussis toxin; sialate; vesicle /vacuole

The binding of pertussis toxin and it B oligomer to lipid vesicles containing glycosphingolipids was studied. Both pertussis toxin and the B oligomer bound to lipid vesicles containing ganglioside GD1a. Binding of pertussis toxin to these vesicles decreased upon treatment of the vesicles with neuraminidase, suggesting that sialic acid residues are important for efficient binding of the toxin to GD1a. These findings are consistent with the idea that sialic acid residues may play a role in efficient pertussis toxin binding to glycolipids. Although the data reported here do not address whether GD1a acts as a functional receptor for PT on the surface of eukaryotic cells, these data provide information concerning the oligosaccharide structures to which PT is capable of binding. The localization of pertussis toxin within wild-type and mutant B. pertussis cells was also studied. Pertussis toxin in both wild-type cells and in mutants deficient in the secretion of the toxin fractionated with the membrane suggesting that pertussis toxin or its subunits may associate loosely with membranes or with proteins localized in the membrane.

百日咳毒素及其B寡聚物与脂囊泡的结合 研究了含有糖鞘脂的物质。 百日咳毒素和 B 寡聚物与含有神经节苷脂 GD1a 的脂质囊泡结合。 装订 经过治疗后，这些囊泡中的百日咳毒素减少了 带有神经氨酸酶的囊泡，表明唾液酸残基 对于毒素与 GD1a 的有效结合很重要。 这些发现是 与唾液酸残基可能发挥作用的观点一致 百日咳毒素与糖脂有效结合。 虽然数据 此处报道并未解决 GD1a 是否充当功能性受体 对于真核细胞表面的PT，这些数据提供了信息 关于 PT 能够形成的寡糖结构 绑定。百日咳毒素在野生型和突变体中的定位 还研究了百日咳博德特氏菌细胞。 两种野生型中的百日咳毒素 细胞和突变体中毒素分馏分泌不足 膜表明百日咳毒素或其亚基可能 与膜或与位于细胞内的蛋白质松散地结合 膜。