Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes
Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes
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DOI：
10.1292/jvms.67.69
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发表时间：
2005-01-01
影响因子：
1.2
通讯作者：
Kozaki, S
中科院分区：
文献类型：
--
作者：
Hang'Ombe, MB;Kohda, T;Kozaki, S
本文测定了多种动物红细胞中败血梭菌α-毒素的活性，其敏感性依次为小鼠、大鼠、犬、马、兔、鸡、牛、猪、羊。温度和酶处理影响红细胞对α-毒素的敏感性。蛋白水解酶K处理降低了小鼠、犬、马和牛红细胞对α-毒素活性的敏感性，但不改变绵羊红细胞对α-毒素活性的敏感性。而猪红细胞经蛋白酶K、胰酶、胰凝乳酶或赖氨酰内肽酶处理后，其α-毒素活性增加。毒素重叠分析表明，在小鼠、马、牛、猪和鸡中，α-毒素与红细胞膜蛋白结合，分子量在30~45 kDa之间；而在大鼠红细胞膜上，α-毒素与100 kDa蛋白发生反应。用磷脂酰肌醇特异性磷脂酶C处理小鼠和猪红细胞膜，可使毒素结合蛋白在天然状态下从单个红细胞膜上释放出来。这些结果表明，α-毒素与任何动物的特定红细胞膜蛋白相结合，并且是不同动物物种中糖基磷脂酰肌醇锚定蛋白的亚群。这些结果可能反映了不同红细胞对α-毒素溶血活性的不同特点。
The activity of Clostridium septicum alpha-toxin was determined in erythrocytes of various animals, with sensitivities observed in the order of mouse, rat, canine, equine, rabbit, chicken, bovine, swine and ovine. Temperature and protease treatment affected the sensitivity of erythrocytes to alpha-toxin. Proteinase K treatment decreased the sensitivity of murine, canine, equine and bovine erythrocytes, but ovine erythrocytes did not change the sensitivity to alpha-toxin activity. On the other hand, the activity of alpha-toxin on swine erythrocytes increased after treatment with proteinase K, trypsin, chymotrypsin or lysyl endopeptidase. Toxin overlay assay showed that alpha-toxin bound to erythrocyte membrane proteins with a molecular mass of 30 to 45-kDa in mouse, equine, bovine, swine and chicken, whereas in rat erythrocyte membranes the toxin reacted with 100-kDa protein. The treatment of murine and swine erythrocyte membranes with phosphatidylinositol-specific phospholipase C resulted in liberation of the toxin-binding protein from the individual membranes in a native state. These results show that alpha-toxin associates with specific erythrocyte membrane proteins in any animal species, and are subsets of glycosylphosphatidylinositol-anchored proteins in various animal species. These results may reflect distinct characteristics of the hemolytic activity of alpha-toxin in response to various erythrocytes.