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Characterization of a recombinant fragment that contains a carbohydrate recognition domain of the filamentous hemagglutinin.

机译:重组片段的表征,该片段含有丝状血凝素的碳水化合物识别结构域。

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The filamentous hemagglutinin (FHA) of Bordetella pertussis plays an important role in establishing infection by attaching the bacteria to the ciliated respiratory epithelial cells. Expression of DNA encoding residues 1141 to 1279 of FHA in Escherichia coli yields a protein of 18,000 Da that exhibits some of the carbohydrate recognition properties of FHA (S. M. Prasad, Y. Yin, E. Rodzinski, E. I. Tuomanen, and H. R. Masure, Infect. Immun. 61:2780-2785, 1993). We have constructed an E. coli strain that expresses this protein, designated fragment A, in a soluble form at markedly elevated levels. Fragment A could be purified with high purity and yields and was immunogenic in mice. Both fragment A and anti-fragment A sera inhibited the binding of B. pertussis to asialo-GM2 and to rabbit ciliated cells. These observations demonstrate that this fragment of FHA contains a cellular binding domain capable of eliciting functional antibodies.
机译:百日咳博德特氏菌的丝状血凝素(FHA)通过将细菌附着在纤毛的呼吸道上皮细胞上,在建立感染中起着重要作用。在大肠杆菌中表达编码FHA残基1141至1279的DNA产生18,000 Da的蛋白质,该蛋白质具有FHA的某些碳水化合物识别特性(SM Prasad,Y.Yin,E.Rodzinski,EI Tuomanen和HR Masure,Infect。 Immun.61:2780-2785,1993)。我们已经构建了一种大肠杆菌菌株,该菌株以可溶形式显着升高的水平表达该蛋白质,称为片段A。片段A可以高纯度和高产率纯化,并且在小鼠中具有免疫原性。片段A和抗片段A血清均抑制百日咳博德特氏菌与脱唾液酸GM2和兔纤毛细胞的结合。这些观察表明,FHA的该片段包含能够引发功能性抗体的细胞结合域。

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