G（F17）菌毛复合体的GafD蛋白赋予大肠杆菌对层粘连蛋白的黏附性。
The GafD protein of the G (F17) fimbrial complex confers adhesiveness of Escherichia coli to laminin.
作者信息
Saarela S, Westerlund-Wikström B, Rhen M, Korhonen T K
机构信息
Department of Biosciences, University of Helsinki, Finland.
出版信息
Infect Immun. 1996 Jul;64(7):2857-60. doi: 10.1128/iai.64.7.2857-2860.1996.
Abstract
Escherichia coli IHE11088(pRR-5) expressing the G (F17) fimbria adhered to immobilized laminin as well as to reconstituted basement membranes. No adhesion was seen with the plasmidless strain IHE11088 or with the deletion derivative IHE11088(pHUB110), which expresses the G-fimbrial filament with a defective GafD lectin and lacks N-acetyl-D-glucosamine-specific binding. Adhesion of IHE11088(pRR-5) to laminin and to reconstituted basement membranes was specifically inhibited by N-acetyl-D-glucosamine, and adhesion was abolished after N-glycosidase F treatment of laminin. The results show that the GafD lectin binds to laminin carbohydrate and suggest a novel function for the F17 fimbria in binding to mammalian basement membranes.
摘要
表达G（F17）菌毛的大肠杆菌IHE11088（pRR - 5）能黏附于固定化的层粘连蛋白以及重组基底膜。无质粒菌株IHE11088或缺失衍生物IHE11088（pHUB110）未见黏附现象，后者表达具有缺陷性GafD凝集素的G菌毛丝且缺乏N - 乙酰 - D - 葡糖胺特异性结合。IHE11088（pRR - 5）对层粘连蛋白和重组基底膜的黏附被N - 乙酰 - D - 葡糖胺特异性抑制，且层粘连蛋白经N - 糖苷酶F处理后黏附作用消失。结果表明，GafD凝集素与层粘连蛋白碳水化合物结合，并提示F17菌毛在结合哺乳动物基底膜方面具有新功能。
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