The Mycoplasma gallisepticum alpha-enolase is cell surface-exposed and mediates adherence by binding to chicken plasminogen

文献类型： 外文期刊

第一作者： Yu, Shengqing

作者： Yu, Shengqing;Ding, Chan;Chen, Hongjun;Yu, Shengqing;Shen, Xinyue;Chen, Danqing;Qiu, Xvsheng;Song, Cuiping;Ding, Chan

作者机构：

关键词： NADH: 58-68-4;plasminogen: 9001-91-6;alpha-enolase: 9014-08-8;EC 4.2.1.11;NAD: 53-84-9;anti-serum;enzyme activity;cell adherence;cell surface

期刊名称：MICROBIAL PATHOGENESIS （ 影响因子：3.738； 五年影响因子：3.663 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The alpha-enolase protein is reported to be an adhesin in several pathogenic bacterial species, but its role in Mycoplasma gallisepticum is unknown. In this study, the M. gallisepticum alpha-enolase gene was adapted to heterologous expression in Escherichia coli by performing overlapping polymerase chain reaction with site-directed mutagenesis to introduce A960G and A1158G mutations in the nucleotide sequence. The full-length mutated gene was cloned into a pGEM-T Easy vector and subcloned into the expression vector pET32a(+) to construct the pET-rMGEno plasmid. The expression of rMGEno in E. coli strain DE3 was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis with Coomassie blue staining. Purified rMGEno exhibited alpha-enolase catalytic activity that it could reflect the conversion of NADH to NAD(+). Mouse antiserum to alpha-enolase was generated by immunization with rMGEno. Immunoblotting and immunofluorescence assay with the antiserum identified alpha-enolase on the surface of M. gallisepticum cells. Enzyme-linked immunosorbent assay characterized rMGEno as a chicken plasminogen binding protein. An adherence inhibition assay on immortalized chicken fibroblasts (DF-1) demonstrated more than 77% inhibition of adhesion in the presence of mouse antiserum, suggesting that alpha-enolase of M. gallisepticum participates in bacterial adhesion to DF-1 cells

分类号： R3

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