Characterization of triosephosphate isomerase from Mycoplasma gallisepticum

被引：10

作者：

Bao, Shijun ^{[1
,2
]}

Chen, Danqing ^{[1
]}

Yu, Shengqing ^{[1
]}

Chen, Hongjun ^{[1
]}

Tan, Lei ^{[1
]}

Hu, Meirong ^{[1
]}

Qiu, Xusheng ^{[1
]}

Song, Cuiping ^{[1
]}

Ding, Chan ^{[1
,3
]}

机构：

[1] Chinese Acad Agr Sci, Shanghai Vet Res Inst, Shanghai 200241, Peoples R China

[2] Gansu Agr Univ, Coll Vet Med, Lanzhou 730070, Peoples R China

[3] Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Peoples R China

来源：

FEMS MICROBIOLOGY LETTERS | 2015年 / 362卷 / 17期

关键词：

Mycoplasma gallisepticum; triosephosphate isomerase; catalytic activity; cytoadherence; ELONGATION-FACTOR TU; NF-KAPPA-B; ALPHA-ENOLASE; STRAIN-R; PARACOCCIDIOIDES-BRASILIENSIS; CYTADHERENCE-DEFICIENT; FIBRONECTIN-BINDING; GLYCOLYTIC ENZYME; PNEUMONIAE; SURFACE;

D O I：

10.1093/femsle/fnv140

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

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.

引用

页数：9

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