Inter J Stomatol ›› 2016, Vol. 43 ›› Issue (3): 273-277.doi: 10.7518/gjkq.2016.03.005

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Differential expression of surface-associated proteins in clinical isolations of Streptococcus mutans

Zhao Xingfu1, Jiang Shan2, Huang Xiaojing2, Yan Fuhua3   

  1. 1. Dept. of Conservative Dentistry and Endodontics II, Tianjin Stomatological Hospital, Stomatological Hospital of Nankai University, Tianjin 300041, China; 2. Dept. of Conservative Dentistry and Endodontics, Hospital of Stomatology, Fujian Medical University, Fuzhou 350002, China; 3. Dept. of Senior Expert Diagnosis and Treatment, Hospital of Stomatology, Medical School of Nanjing University, Nanjing 210008, China) This study was supported by the National Natural Science Foundation of China(30500564).
  • Received:2015-06-12 Revised:2015-11-16 Online:2016-05-01 Published:2016-05-01

Abstract: Objective This study aims to investigate the changes in the expression of surface-associated protein at pH7.0 in Streptococcus mutans isolated from clinical samples. Methods The proteins were extracted from the cells at pH7.0 by using the Homer method. The proteins were separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis(SDSPAGE) and 2D gel electrophoresis(2DE) followed by image analysis. The proteins were identified by matrix-assisted laser desorption time of flight(MALDI-TOF) mass spectrometry and computer-assisted protein sequence analysis. Results Image analysis revealed that 14 high expression protein loci and 8 specific protein loci exist in Streptococcus mutans 593. Specifically, pyruvate kinase and adenosine triphosphate-binding cassette transporter were modulated, and glucose transferase was highly modulated in Streptococcus mutans 593. Conclusion The difference in protein expression of the two clinical isolations may indicate their distinct cariogenic characters.

Key words: Streptococcus mutans, proteomics, clinical isolation, surface-associated protein, Streptococcus mutans, proteomics, clinical isolation, surface-associated protein

CLC Number: 

  • Q 51

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