Mills S D, Bradbury W C, Penner J L
J Clin Microbiol. 1986 Jul;24(1):69-75. doi: 10.1128/jcm.24.1.69-75.1986.
Flagellin protein was isolated and purified from two serotype reference strains of Campylobacter jejuni, Pen 1 and Pen 3. Each preparation was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis to consist of a diffuse band with a molecular mass of approximately 62 kilodaltons. Antisera were prepared against flagellin from Pen 1, and specific antibody was isolated by affinity chromatography with flagellin protein covalently bound to cyanogen bromide-activated Sepharose. The high-affinity antibody was used to immune blot purified flagellin from Pen 1 and Pen 3, as well as whole-cell preparations and acid-glycine extracts from the 60 reference strains of the thermostable antigen serotyping system. From each of the 60 strains, a protein with a molecular mass of approximately 62 kilodaltons was identified which shared a common antigenic determinant. When the affinity-purified antibody was used in a coagglutination assay, washed whole cells were not agglutinable unless they had been pretreated with an acid buffer (glycine-hydrochloride [pH 2.0]). This indicated that the antigenic determinant common to strains of both C. jejuni and Campylobacter coli may not be exposed in the native state.
从空肠弯曲菌的两个血清型参考菌株Pen 1和Pen 3中分离并纯化鞭毛蛋白。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示，每种制剂均由一条弥散带组成，其分子量约为62千道尔顿。制备了针对Pen 1鞭毛蛋白的抗血清，并通过用与溴化氰活化的琼脂糖共价结合的鞭毛蛋白进行亲和层析来分离特异性抗体。高亲和力抗体用于免疫印迹Pen 1和Pen 3的纯化鞭毛蛋白，以及热稳定抗原血清分型系统的60个参考菌株的全细胞制剂和酸-甘氨酸提取物。从60个菌株中的每一个中，都鉴定出一种分子量约为62千道尔顿的蛋白质，它们具有共同的抗原决定簇。当在协同凝集试验中使用亲和纯化的抗体时，除非用酸缓冲液（甘氨酸-盐酸[pH 2.0]）预处理，否则洗涤后的全细胞不会发生凝集。这表明空肠弯曲菌和结肠弯曲菌菌株共有的抗原决定簇在天然状态下可能未暴露。
