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Characterization of Triosephosphate Isomerase From Mycoplasma Gallisepticum

Characterization of Triosephosphate Isomerase From Mycoplasma Gallisepticum

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

FEMS Microbiol Lett. 2015 Sep;362(17):fnv140.

PMID: 26319024

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9023783-B	Triosephosphate Isomerase from rabbit muscle		9023-78-3	Price

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