Hranitzky K W, Mulholland A, Larson A D, Eubanks E R, Hart L T
Infect Immun. 1980 Feb;27(2):597-603. doi: 10.1128/iai.27.2.597-603.1980.
A flagellar sheath protein of Vibrio cholerae CA401 (Inaba) was characterized. Purity of the preparation was indicated by a single band on polyacrylamide gel electrophoresis gels and on Ouchterlony plates prepared with antibody against crude sheath material. The sheath protein was composed of three polypeptides with minimal molecular weights of 61,500, 60,000, and 56,500. The presence of sheath protein on the flagellum as well as on the outer membrane of the cell was demonstrated by ferritin labeling experiments with antiserum. Sheath protein antibody reacted similarly in labeling experiments and agglutination tests with a classical Ogawa strain and two nonagglutinating V. cholerae isolates, indicating that the sheath protein may represent the common Vibrio H antigen. Antibody specific for lipopolysaccharide labeled the cell but not the sheathed flagellum, which demonstrated that the sheath is not a simple extension of the outer membrane of the cell.
对霍乱弧菌CA401（稻叶型）的一种鞭毛鞘蛋白进行了特性分析。聚丙烯酰胺凝胶电泳凝胶以及用抗粗鞘材料抗体制备的双向免疫扩散板上的单一条带表明了制备物的纯度。鞘蛋白由三种多肽组成，其最小分子量分别为61,500、60,000和56,500。用抗血清进行的铁蛋白标记实验证明了鞭毛以及细胞外膜上存在鞘蛋白。鞘蛋白抗体在标记实验和凝集试验中与一株典型小川型菌株及两株非凝集性霍乱弧菌分离株的反应相似，这表明鞘蛋白可能代表常见的弧菌H抗原。脂多糖特异性抗体标记了细胞，但未标记带鞘鞭毛，这表明鞘不是细胞外膜的简单延伸。
