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（PIyWT） and PIyM2 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 PIyWT and Streptococcus pneumoniae（S, pneumoniae）. These results give support to PIyM2 to be a new protein antigen for inclusion in the development of an effective pneumocoecal multiprotein vaccine.
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（PIyWT） and PIyM2 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 PIyWT and Streptococcus pneumoniae（S, pneumoniae）. These results give support to PIyM2 to be a new protein antigen for inclusion in the development of an effective pneumocoecal multiprotein vaccine.
