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高等学校化学研究 ›› 2015, Vol. 31 ›› Issue (4): 553-557.doi: 10.1007/s40242-015-5105-3

• Articles • 上一篇    下一篇

Detection and Comparison of Structure and Function of Wild-type Pneumolysin and Its Novel Mutant PlyM2

SUN Tianxu, HOU Hongjia, LU Jingcai, XU Man, GU Tiejun, WANG Dandan, DONG Yunliang, JIANG Chunlai, KONG Wei, WU Yongge   

  1. National Engineering Laboratory for Aids Vaccine, School of Life Science, Jilin University, Changchun 130012, P. R. China
  • 收稿日期:2015-03-17 修回日期:2015-04-03 出版日期:2015-08-01 发布日期:2015-06-08
  • 通讯作者: WU Yongge E-mail:yonggewu@163.com

Detection and Comparison of Structure and Function of Wild-type Pneumolysin and Its Novel Mutant PlyM2

SUN Tianxu, HOU Hongjia, LU Jingcai, XU Man, GU Tiejun, WANG Dandan, DONG Yunliang, JIANG Chunlai, KONG Wei, WU Yongge   

  1. National Engineering Laboratory for Aids Vaccine, School of Life Science, Jilin University, Changchun 130012, P. R. China
  • Received:2015-03-17 Revised:2015-04-03 Online:2015-08-01 Published:2015-06-08
  • Contact: WU Yongge E-mail:yonggewu@163.com

摘要:

Here is reported a novel pneumolysin(Ply) mutant(PlyM2) that addresses a long-standing problem for vaccine development in this field: detoxification of Ply in the premise of retaining antigenic integrity. Structure and function of wild-type Ply(PlyWT) and PlyM2 mutants were detected and compared. Their structures were not signi- ficantly different according to the analysis by thermal-dependent fluorescence spectroscopy and circular dichroism spectroscopy. PlyM2 was confirmed to have lost hemolytic activity and yet could induce neutralizing antibodies to prevent in vitro hemolysis by PlyWT and Streptococcus pneumoniae(S. pneumoniae). These results give support to PlyM2 to be a new protein antigen for inclusion in the development of an effective pneumococcal multiprotein vaccine.

关键词: Pneumolysin, Circular dichroism spectroscopy, Thermal-dependent fluorescence spectroscopy, Streptococcus pneumoniae, Detoxification, Mutation

Abstract:

Here is reported a novel pneumolysin(Ply) mutant(PlyM2) that addresses a long-standing problem for vaccine development in this field: detoxification of Ply in the premise of retaining antigenic integrity. Structure and function of wild-type Ply(PlyWT) and PlyM2 mutants were detected and compared. Their structures were not signi- ficantly different according to the analysis by thermal-dependent fluorescence spectroscopy and circular dichroism spectroscopy. PlyM2 was confirmed to have lost hemolytic activity and yet could induce neutralizing antibodies to prevent in vitro hemolysis by PlyWT and Streptococcus pneumoniae(S. pneumoniae). These results give support to PlyM2 to be a new protein antigen for inclusion in the development of an effective pneumococcal multiprotein vaccine.

Key words: Pneumolysin, Circular dichroism spectroscopy, Thermal-dependent fluorescence spectroscopy, Streptococcus pneumoniae, Detoxification, Mutation