THE PAPG PROTEIN IS THE ALPHA-D-GALACTOPYRANOSYL-(1-]4)-BETA-D-GALACTOPYRANOSE-BINDING ADHESIN OF UROPATHOGENIC ESCHERICHIA-COLI

THE PAPG PROTEIN IS THE ALPHA-D-GALACTOPYRANOSYL-(1-]4)-BETA-D-GALACTOPYRANOSE-BINDING ADHESIN OF UROPATHOGENIC ESCHERICHIA-COLI
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DOI:
10.1073/pnas.84.16.5898
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发表时间:
1987-08-01
影响因子:
11.1
通讯作者:
NORMARK, S
NORMARK, S
中科院分区:
综合性期刊1区
文献类型:
--
作者:
LUND, B;LINDBERG, F;NORMARK, S

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尿路致病性大肠杆菌通过其二半乳糖苷 .α.-D-吡喃半乳糖基-(1 .fwdarw. 4)-.beta.-D-吡喃半乳糖 [a-D-Galp-(1 .fwdarw. 4)-.beta.-D-Galp 或 Gal.alpha.(1 .fwdarw. 4)Gal] 粘附在尿路上皮细胞上,结合菌毛,由重复的相同亚基组成。这些菌毛的主要亚基 (PapA) 不是结合所必需的,但 papF 和 papG 基因产物对于粘附是必需的。 pap基因簇和编码不同结合特异性的相关基因簇之间的反式互补分析表明,PapG而不是PapF是Gal.alpha。 (1.fwdarw.4)Gal 特异性粘附素。用完整的巴氏菌毛免疫获得了针对 PapG 的抗体,表明粘附素是菌毛成分。使用针对不同 Pap 蛋白的特异性抗血清来证明菌毛蛋白(PapA 或 PapE)以及 PapG 和 PapF 必须暴露在细胞表面才能允许大肠杆菌结合。给出了 papG 基因的 DNA 序列,推导的一级结构显示出与双半乳糖苷结合志贺氏菌毒素的 B 链序列的相似性,并建立了菌毛蛋白的氨基酸序列。
Uropathogenic Escherichia coli adhere to uroepithelial cells by their digalactoside .alpha.-D-galactopyranosyl-(1 .fwdarw. 4)-.beta.-D-galactopyranose [a-D-Galp-(1 .fwdarw. 4)-.beta.-D-Galp or Gal.alpha.(1 .fwdarw. 4)Gal], binding pilli, which are composed of repeating identical subunits. The major subunit (PapA) of these pili is not required for binding, but the papF and papG gene products are essential for adhesion. Transcomplementation analysis between the pap gene cluster and a related gene cluster encoding a different binding specificity showed that PapG and not PapF is the Gal.alpha. (1 .fwdarw. 4)Gal-specific adhesin. Antibodies against PapG were obtained upon immunizing with whole Pap pili, showing that the adhesin is a pilus component. Antisera specific for different Pap proteins were used to demonstrate that a pilin protein, either PapA or PapE, together with both PapG and PapF, must be exposed on the cell surface to allow E. coli to bind. The DNA sequence of the papG gene is presented, and the deduced primary structure showed similarities both to the B-chain sequence of the digalactoside-binding Shigella toxin and to establish amino acid sequences of pilins.