Chinese Journal of Tissue Engineering Research ›› 2010, Vol. 14 ›› Issue (46): 8643-.doi: 10.3969/j.issn.1673-8225.2010.46.022

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Effects of peptidoglycan acetylation in Neisseria gonorrhoeae on catalysis activity of murein lytic transglycosylase A from E. coli

Wu Teng-fei, Zhang Qiao-ling, Deng Xu-ming, Liu Bo   

  1. Laboratory of Basic Veterinary Medicine, College of Animal Sciences and Veterinary Medicine, Jilin University, Changchun  130062, Jilin Province, China
  • Online:2010-11-12 Published:2010-11-12
  • Contact: Liu Bo, Professor, Doctoral supervisor, Laboratory of Basic Veterinary Medicine, College of Animal Sciences and Veterinary Medicine, Jilin University, Changchun 130062, Jilin Province, China Liuboy@hotmail.com
  • About author:Wu Teng-fei☆, Doctor, Laboratory of Basic Veterinary Medicine, College of Animal Sciences and Veterinary Medicine, Jilin University, Changchun 130062, Jilin Province, China Tengfei_Wu@yahoo.com
  • Supported by:

    the National Natural Science Foundation of China, No. 30972170*; Scientific Frontier and Cross-Disciplinary Innovation Item, No. 200903337*

Abstract:

BACKGROUND: Studies have demonstrated that E. coli peptidoglycan (PG) acetylation suppresses catalysis activity of lytic transglycosylase. However, whether PG acetylation in Neisseria gonorrhoeae (N. gonorrhoeae) has the same effect remains poorly understood.
OBJECTIVE: To identify effect of PG acetylation in N. gonorrhoeae on catalysis activity of lytic transglycosylase family 2 in gram-negative bacteria.
METHODS: PG acetylation genes (pacAB) in N. gonorrhoeae FA19 were knocked out though transformation by homologous recombination. 3H-glucosamine labeled PG from either wild type N. gonorrhoeae FA19 (PG1) or pacAB mutant strain (PG2) were isolated respectively. We amplified, cloned, expressed and purified lytic transglycosylase (MltA) from E. coli. The catalysis activity of MltA on PG1 and PG2 was detected, and the optimum reaction temperature was measured.
RESULTS AND CONCLUSION: The recombinant MltA was obtained at the concentration of 26.12 g/mL. Only 9.71% PG1 was cleaved, but around 93.45% of no-acetylation PG2 was cleaved. The optimum reaction temperature was 30 ℃. PG with O-acetylation decreased catalysis capability of MltA. It suggests acetylation of PG in N gonorrhoeae inhibited the autolysis caused by MltA.

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