Kobayashi Y, Ohta H, Kokeguchi S, Murayama Y, Kato K, Kurihara H, Fukui K
Department of Periodontology and Endodontology, Okayama University Dental School, Japan.
FEMS Microbiol Lett. 1993 Apr 15;108(3):275-80. doi: 10.1111/j.1574-6968.1993.tb06115.x.
The antigenic properties of the surface layer (S-layer) proteins of various Campylobacter rectus strains including 24 clinical isolates and the type strain ATCC 33238 were examined. S-layer proteins were extracted from whole cells by acid treatment according to the method of McCoy et al. (Infect. Immun. 11, 517-525, 1975). The acid extracts from 23 of the isolates and ATCC 33238 contained two major proteins with molecular masses of 130 kDa and 150 kDa, both of which were identified as subunits of the S-layer after comparison with the protein profiles of acid-treated (S-layer-deficient) cells. An S-layer protein from one isolate (CI-808) demonstrated a different molecular mass (160 kDa). Both the 150-kDa proteins of ATCC 33238 and isolate CI-306 and the 160-kDa protein of CI-808 were purified by ion-exchange chromatography in the presence of urea. In Ouchterlony immunodiffusion experiments with these purified proteins and rabbit antiserum raised to each purified protein, both common and strain-specific antigenic determinants were identified in the C. rectus S-layer proteins.
对包括24株临床分离株和模式菌株ATCC 33238在内的多种直肠弯曲菌菌株的表面层（S层）蛋白的抗原特性进行了检测。根据McCoy等人（《感染与免疫》11，517 - 525，1975年）的方法，通过酸处理从全细胞中提取S层蛋白。23株分离株和ATCC 33238的酸提取物含有两种主要蛋白质，分子量分别为130 kDa和150 kDa，与酸处理（S层缺陷）细胞的蛋白质谱比较后，这两种蛋白质均被鉴定为S层的亚基。一株分离株（CI - 808）的S层蛋白显示出不同的分子量（160 kDa）。ATCC 33238和分离株CI - 306的150 kDa蛋白以及CI - 808的160 kDa蛋白在尿素存在下通过离子交换色谱法进行了纯化。在使用这些纯化蛋白和针对每种纯化蛋白产生的兔抗血清进行的双向免疫扩散实验中，在直肠弯曲菌S层蛋白中鉴定出了共同和菌株特异性抗原决定簇。
