Babai R, Stern B E, Hacker J, Ron E Z
Department of Molecular Microbiology and Biotechnology, Faculty of Life Sciences, Tel-Aviv University, Tel-Aviv, Israel.
Infect Immun. 2000 Oct;68(10):5901-7. doi: 10.1128/IAI.68.10.5901-5907.2000.
Fimbrial adhesins that mediate attachment to host cells are produced by most virulent Escherichia coli isolates. These virulence factors play an important role in the initial stages of bacterial colonization and also in determination of the host and tissue specificity. Isolates belonging to serotype O78 are known to cause a large variety of clinical syndromes in farm animals and humans and have been shown to produce several types of adherence fimbriae. We studied the fimbrial adhesin from an avian septicemic E. coli isolate of serotype O78. Analysis of the genetic organization of the fac (fimbria of avian E. coli) gene cluster indicates that it belongs to the S-fimbrial adhesin family. Seven open reading frames coding for major and minor structural subunits were identified, and most of them showed a high degree of homology to the corresponding Sfa and Foc determinants. The least-conserved open reading frame was facS, encoding a protein known to play an important role in determining adherence specificity in other S-fimbrial gene clusters.
大多数致病性大肠杆菌分离株都会产生介导与宿主细胞附着的菌毛黏附素。这些毒力因子在细菌定植的初始阶段以及宿主和组织特异性的决定中都起着重要作用。已知属于血清型O78的分离株会在农场动物和人类中引起多种临床综合征,并且已证明它们会产生几种类型的黏附菌毛。我们研究了一株血清型O78的禽败血性大肠杆菌分离株的菌毛黏附素。对fac(禽大肠杆菌菌毛)基因簇的遗传组织分析表明,它属于S菌毛黏附素家族。鉴定出了七个编码主要和次要结构亚基的开放阅读框,其中大多数与相应的Sfa和Foc决定簇具有高度同源性。保守性最低的开放阅读框是facS,它编码一种已知在其他S菌毛基因簇中决定黏附特异性方面起重要作用的蛋白质。