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首页> 外文期刊>Journal of bacteriology >Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene.
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Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene.

机译：跟踪细菌胆碱结合域的演变：丙酮丁醇梭菌NCIB 8052 cspA基因的分子表征。

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摘要

The major secreted protein of Clostridium acetobutylicum NCIB 8052, a choline-containing strain, is CspA (clostridial secreted protein). It appears to be a 115,000-M(r) glycoprotein that specifically recognizes the choline residues of the cell wall. Polyclonal antibodies raised against CspA detected the presence of the protein in the cell envelope and in the culture medium. The soluble CspA protein has been purified, and an oligonucleotide probe, prepared from the determined N-terminal sequence, has been used to clone the cspA gene which encodes a protein with 590 amino acids and an M(r) of 63,740. According to the predicted amino acid sequence, CspA is synthesized with an N-terminal segment of 26 amino acids characteristic of prokaryotic signal peptides. Expression of the cspA gene in Escherichia coli led to the production of a major anti-CspA-labeled protein of 80,000 Da which was purified by affinity chromatography on DEAE-cellulose. A comparison of CspA with other proteins in the EMBL database revealed that the C-terminal half of CspA is homologous to the choline-binding domains of the major pneumococcal autolysin (LytA amidase), the pneumococcal antigen PspA, and other cell wall-lytic enzymes of pneumococcal phages. This region, which is constructed of four repeating motifs, also displays a high similarity with the glucan-binding domains of several streptococcal glycosyltransferases and the toxins of Clostridium difficile.
机译：含胆碱的菌株丙酮丁醇梭菌NCIB 8052的主要分泌蛋白是CspA（梭菌分泌蛋白）。它似乎是一种115,000-M（r）糖蛋白，可以特异性识别细胞壁的胆碱残基。产生针对CspA的多克隆抗体可检测到细胞膜和培养基中蛋白质的存在。已纯化了可溶性CspA蛋白，并使用从确定的N端序列制备的寡核苷酸探针克隆了cspA基因，该基因编码具有590个氨基酸的蛋白，M（r）为63,740。根据预测的氨基酸序列，合成具有原核信号肽特征的26个氨基酸的N末端区段的CspA。 cspA基因在大肠杆菌中的表达导致产生了80,000 Da的主要抗CspA标记蛋白，该蛋白通过DEAE-纤维素亲和层析纯化。 CspA与EMBL数据库中其他蛋白质的比较显示，CspA的C末端一半与主要的肺炎球菌自溶素（LytA酰胺酶），肺炎球菌抗原PspA和其他细胞壁分解酶的胆碱结合域同源肺炎球菌噬菌体。该区域由四个重复的基序构成，也与几种链球菌糖基转移酶的葡聚糖结合结构域和艰难梭菌毒素具有高度相似性。

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