Characterization of triosephosphate isomerase from Mycoplasma gallisepticum

文献类型： 外文期刊

第一作者： Bao, Shijun

作者： Bao, Shijun;Chen, Danqing;Yu, Shengqing;Chen, Hongjun;Tan, Lei;Hu, Meirong;Qiu, Xusheng;Song, Cuiping;Ding, Chan;Bao, Shijun;Ding, Chan

作者机构：

关键词： Mycoplasma gallisepticum;triosephosphate isomerase;catalytic activity;cytoadherence

期刊名称：FEMS MICROBIOLOGY LETTERS （ 影响因子：2.742； 五年影响因子：2.856 ）

ISSN： 0378-1097

年卷期： 2015 年 362 卷 17 期

页码：

收录情况： SCI

摘要： Triosephosphate isomerase (Tpi) is a glycolytic enzyme that is essential for efficient energy production in many pathogens. However, its function in Mycoplasma gallisepticum has not been fully elucidated. In this study, the mga0357 gene of M. gallisepticum, which encodes TpiA (MGTpiA), was amplified and expressed in Escherichia coli by IPTG induction. The purified recombinant MGTpiA protein exhibited catalytic activity that was similar to TPI from rabbit muscle, reducing NAD+ to NADH. The MGTpiA was also found to be a surface-exposed protein by western blotting and immunofluorescence assays. In addition, cytadherence inhibition assays confirmed that the cytadherence of M. gallisepticum to the DF-1 cells was significantly inhibited by the anti-MGTpiA serum. The results of the study suggested that MGTpiA plays an important role in the metabolism and closely related to the M. gallisepticum pathogenicity.

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