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首页> 外文期刊>Infection and immunity >The central variable V2 region of the CS31A major subunit is involved in the receptor-binding domain.
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The central variable V2 region of the CS31A major subunit is involved in the receptor-binding domain.

机译：CS31A主要亚基的中央可变V2区参与受体结合域。

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CS31A is a K88-related capsule-like surface protein that mediates Escherichia coli and Klebsiella pneumoniae adhesion to the human Caco-2 and Intestine-407 cell lines. In this study, we demonstrate that ClpG, the major subunit of CS31A, contains the adhesive domain of the polymerized structure. We mapped this domain within the ClpG protein by performing adhesion inhibition experiments with Intestine-407 cells with nine synthetic peptides (CLP1 to CLP9) covering the dominant antigenic regions of ClpG and with the corresponding rabbit antipeptide antibodies. The peptides CLP1 (amino acid positions in parentheses) (5-18), CLP2 (44-56), CLP3 (82-96), CLP7 (174-190), CLP8 (185-199), and CLP9 (235-249) and corresponding antipeptide antibodies targeting parts of the N- and C-terminal regions of ClpG had no effect on the adhesion of the TCFF15 recombinant strain expressing CS31A. Only the CLP5 (132-146) peptide, corresponding to the central part of the protein, and relevant antibodies inhibited bacterial adhesion to intestinal epithelial cells. Anti-CLP4 (97-109) and anti-CLP6 (148-162) antibodies targeting regions surrounding the CLP5 sequence also inhibited bacterial adhesion. Site-directed mutagenesis experiments inducing changes in the amino acid sequence of the ClpG protein corresponding to the CLP5 peptide resulted in the expression of nonadhesive CS31A antigen. These findings indicate that the ClpG receptor-binding domain is located in the central variable V2 region.
机译：CS31A是一种K88相关的胶囊样表面蛋白，可介导大肠杆菌和肺炎克雷伯菌对人Caco-2和Intestine-407细胞系的粘附。在这项研究中，我们证明ClpG，CS31A的主要亚基，包含聚合结构的粘合域。我们通过对肠道407细胞进行粘着抑制实验来绘制ClpG蛋白内的这个结构域，该细胞具有覆盖ClpG主要抗原区域的九种合成肽（CLP1至CLP9）以及相应的兔抗肽抗体。肽CLP1（括号中的氨基酸位置）（5-18），CLP2（44-56），CLP3（82-96），CLP7（174-190），CLP8（185-199）和CLP9（235-249） ）和靶向ClpG N端和C端区域部分的相应抗肽抗体，对表达CS31A的TCFF15重组菌株的粘附没有影响。仅对应于蛋白质中心部分的CLP5（132-146）肽和相关抗体抑制细菌粘附于肠上皮细胞。靶向CLP5序列周围区域的抗CLP4（97-109）和抗CLP6（148-162）抗体也抑制细菌粘附。定点诱变实验诱导对应于CLP5肽的ClpG蛋白的氨基酸序列发生变化，从而导致了非粘附性CS31A抗原的表达。这些发现表明，ClpG受体结合域位于中央可变V2区域。

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