NeuA O-acetylesterase activity is specific for CMP-activated O-acetyl sialic acid in Streptococcus suis serotype 2.

Lili Song, Hui Zhou, Xuehui Cai, Chunyang Li, Jingnan Liang, Cheng Jin

Key Laboratory of Systematic Mycology and Lichenology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.

Biochemical and biophysical research communications 2011 Jul 1

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Several bacteria causing meningitis, such as Escherichia coli K1, Streptococcus suis, Neisseria meningitidis, and group B Streptococci (GBS), produce sialic acid (Neu5Ac)-containing capsular polysaccharide (CPS). Biosynthesis of the Neu5Ac-containing CPS requires CMP-Neu5Ac as substrate, which is synthesized by CMP-Neu5Ac synthetase from CTP and Neu5Ac. In E. coli or GBS, the NeuA protein encoded by the neuA gene has been known encoding a bifunctional enzyme that possesses both CMP-Neu5Ac synthetase and O-acetylesterase activity. In this report, we found that the S. suis NeuA (SsNeuA) was also a bifunctional CMP-Neu5Ac synthetase/O-acetylesterase. Biochemical analyses revealed that the SsNeuA strictly de-O-acetylated CMP-O-acetyl-Neu5Ac, whereas the E. coli NeuA (EcNeuA) preferentially de-O-acetylated CMP-O-acetyl-Neu5Ac. E. coli devoid of NeuA O-acetylesterase activity was unable to produce capsule and only CMP-Neu5Ac synthetase activity of the EcNeuA or SsNeuA could not restore its ability to produce capsule. These results suggest that the O-acetylesterase is essential for the synthesis of capsular Neu5Ac in E. coli, probably in S. suis and GBS as well. Our findings are key to understanding the biosynthesis of capsular Neu5Ac in E. coli, S. suis and GBS. Copyright © 2011 Elsevier Inc. All rights reserved.

Citation

Lili Song, Hui Zhou, Xuehui Cai, Chunyang Li, Jingnan Liang, Cheng Jin. NeuA O-acetylesterase activity is specific for CMP-activated O-acetyl sialic acid in Streptococcus suis serotype 2. Biochemical and biophysical research communications. 2011 Jul 1;410(2):212-7