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首页> 外文期刊>Journal of bacteriology >The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine.
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The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine.

机译：大肠杆菌G-纤维凝集素蛋白参与纤维生物发生和受体N-乙酰基-D-葡萄糖胺的识别。

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摘要

The gafD gene encoding the N-acetyl-D-glucosamine-specific fimbrial lectin (adhesin) protein GafD of uropathogenic Escherichia coli was cloned and subjected to genetic analysis. The corresponding gene product was isolated as a MalE fusion protein. The lectin gene was identified with the aid of deletion mutagenesis; mutations in gafD impaired either receptor binding or both receptor binding and fimbria production, depending on the mutation created. All mutants converted to wild-type expressors when complemented in trans with the cloned intact gafD gene. The predicted 354-amino-acid sequence of GafD, deduced from the nucleotide sequence, is closely related to those of the fimbria-associated F17-G and F17b-G proteins coded for by enterotoxigenic and invasive E. coli strains. Isolated GafD was shown to recognize N-acetyl-D-glucosamine by virtue of specific binding to an immobilized receptor, thus proving directly that GafD is a sugar-binding protein. Our results indicate that GafD as such is sufficient for receptor recognition and that the protein also participates in fimbrial biogenesis.
机译：克隆了编码尿路致病性大肠杆菌的N-乙酰基-D-氨基葡萄糖特异性纤维凝集素（粘附素）蛋白GafD的gafD基因，并进行了遗传分析。分离出相应的基因产物，作为MalE融合蛋白。凝集素基因借助缺失诱变进行鉴定。 gafD突变会损害受体结合或受体结合和菌毛生成，具体取决于所产生的突变。当与克隆的完整gafD基因反式互补时，所有突变体均转化为野生型表达体。由核苷酸序列推导的GafD预测的354个氨基酸序列与产肠毒素和侵入性大肠杆菌菌株编码的与菌毛相关的F17-G和F17b-G蛋白的序列密切相关。分离出的GafD通过与固定的受体特异性结合而显示出识别N-乙酰基-D-葡糖胺的能力，因此直接证明了GafD是糖结合蛋白。我们的结果表明，GafD本身足以用于受体识别，并且该蛋白质还参与了纤维生物发生。

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