Moser I, Schroeder W, Salnikow J
Institut für Mikrobiologie und Tierseuchen, Freie Universität Berlin, Germany.
FEMS Microbiol Lett. 1997 Dec 15;157(2):233-8. doi: 10.1111/j.1574-6968.1997.tb12778.x.
Campylobacter jejuni is one of the major causes of human diarrhea throughout the world. Attachment to host cells and extracellular matrix proteins is considered to be an essential primary event in the pathogenesis of enteritis. Outer membrane proteins of three C. jejuni strains, one of which was aflagellate, were investigated for their contribution to the process of adhesion to INT 407 cell membranes and the extracellular matrix protein fibronectin. Using a ligand-binding immunoblotting assay the flagellin, the major outer membrane protein and a 59-kDa protein were detected to be involved in adhesion to both substrates. The MOMP was able to inhibit the attachment of the bacteria to INT 407 cell membranes partly, when the protein was isolated under native conditions. However, it was totally lost when the protein was isolated in the presence of SDS. The 59-kDa protein of one strain was identified by N-terminal sequencing, and regarding the first 14 amino acids it was found to be identical to the 37-kDa CadF protein just recently described as fibronectin-binding protein of C. jejuni. Especially for the aflagellate strain this protein may be of special importance for adhesion of the bacteria to different substrates.
空肠弯曲菌是全球人类腹泻的主要病因之一。附着于宿主细胞和细胞外基质蛋白被认为是肠炎发病机制中必不可少的首要事件。研究了三株空肠弯曲菌的外膜蛋白（其中一株为无鞭毛菌株）对INT 407细胞膜和细胞外基质蛋白纤连蛋白的黏附过程的作用。使用配体结合免疫印迹分析，检测到鞭毛蛋白、主要外膜蛋白和一种59 kDa蛋白参与了对两种底物的黏附。当在天然条件下分离该蛋白时，主要外膜蛋白能够部分抑制细菌对INT 407细胞膜的附着。然而，当在SDS存在的情况下分离该蛋白时，其活性完全丧失。通过N端测序鉴定了一株菌株的59 kDa蛋白，就前14个氨基酸而言，发现它与最近被描述为空肠弯曲菌纤连蛋白结合蛋白的37 kDa CadF蛋白相同。特别是对于无鞭毛菌株，这种蛋白可能对细菌黏附于不同底物具有特殊重要性。
