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首页> 外文期刊>Infection and immunity >A neuraminidase from Streptococcus pneumoniae has the features of a surface protein.
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A neuraminidase from Streptococcus pneumoniae has the features of a surface protein.

机译：来自肺炎链球菌的神经氨酸酶具有表面蛋白的特征。

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A gene from Streptococcus pneumoniae (nanA), with features entirely consistent with a neuraminidase gene, has been sequenced. High levels of neuraminidase activity were obtained after cloning of this gene, without flanking sequences, into a high-expression vector. RNA hybridization studies have shown that the gene is transcribed by a virulent pneumococcus strain. The predicted molecular weight of the protein and certain amino acid sequences are typical of other neuraminidases. NanA contains the four copies of the sequence SXDXGXTW that is present in all the bacterial neuraminidases previously described. Kyte and Doolittle analysis showed that NanA is a hydrophilic protein with hydrophobic domains at the N terminus and the C terminus. A putative signal peptide was found in the N terminus of this protein, indicating that the protein is exported from the pneumococcus. The C terminus has the features of the anchor motif found in other surface proteins from gram-positive bacteria. Electron microscopy studies showed the presence of neuraminidase associated with the cell surface of the pneumococcus.
机译：已对来自肺炎链球菌（nanA）的基因进行了测序，该基因的特征与神经氨酸酶基因完全一致。将这个基因（无侧翼序列）克隆到高表达载体中后，获得了高水平的神经氨酸酶活性。 RNA杂交研究表明，该基因被强力肺炎球菌菌株转录。蛋白质的预测分子量和某些氨基酸序列是其他神经氨酸酶的典型特征。 NanA包含序列SXDXGXTW的四个副本，该序列存在于先前描述的所有细菌神经氨酸酶中​​。 Kyte和Doolittle分析表明NanA是一种亲水蛋白，在N端和C端带有疏水域。在该蛋白的N末端发现了一个推定的信号肽，表明该蛋白从肺炎球菌中输出。 C末端具有在革兰氏阳性细菌的其他表面蛋白中发现的锚定基序的特征。电子显微镜研究表明，与肺炎球菌细胞表面有关的神经氨酸酶存在。

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