Characterization of triosephosphate isomerase from Mycoplasma gallisepticum.

Authors :: Bao S
Chen D
Yu S
Chen H
Tan L
Hu M
Qiu X
Song C
Ding C
Source :: FEMS microbiology letters [FEMS Microbiol Lett] 2015 Sep; Vol. 362 (17), pp. fnv140. Date of Electronic Publication: 2015 Aug 27.
Publication Year :: 2015
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.<br /> (© FEMS 2015. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.)