Lindberg F P, Lund B, Normark S
EMBO J. 1984 May;3(5):1167-73. doi: 10.1002/j.1460-2075.1984.tb01946.x.
Most pyelonephritic Escherichia coli strains bind to digalactoside-containing glycolipids on uroepithelial cells. Purified Pap pili (pili associated with pyelonephritis) show the same binding specificity. A non-polar mutation early in the papA pilin gene abolishes formation of Pap pili but does not affect the degree of digalactoside-specific hemagglutination. Three novel pap genes, papE , papF and papG are defined in this report. The papF and papG gene products are both required for digalactoside-specific agglutination by whole bacteria cells as well as for agglutination by pilus preparations. Pili prepared from a papE mutant have lost their binding ability although whole cells from this mutant retain it, implying an adhesin anchoring role for the papE gene product. A mutant with lesions both in the papA and the papE genes does not mediate digalactoside-specific agglutination. The implications of this finding for pilus biogenesis are discussed.
大多数肾盂肾炎大肠杆菌菌株可与尿路上皮细胞上含二半乳糖苷的糖脂结合。纯化的P菌毛（与肾盂肾炎相关的菌毛）显示出相同的结合特异性。papA菌毛蛋白基因早期的一个非极性突变可消除P菌毛的形成，但不影响二半乳糖苷特异性血凝的程度。本报告中定义了三个新的pap基因，即papE、papF和papG。papF和papG基因产物对于全细菌细胞的二半乳糖苷特异性凝集以及菌毛制剂的凝集都是必需的。从papE突变体制备的菌毛失去了其结合能力，尽管该突变体的全细胞仍保留这种能力，这意味着papE基因产物具有粘附素锚定作用。在papA和papE基因中均有损伤的突变体不介导二半乳糖苷特异性凝集。本文讨论了这一发现对菌毛生物发生的影响。
