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Detection and comparison of structure and function of wild-type pneumolysin and its novel mutant PlyM2
Ist Teil von
Chemical research in Chinese universities, 2015-08, Vol.31 (4), p.553-557
Ort / Verlag
Changchun: Jilin University and The Editorial Department of Chemical Research in Chinese Universities
Erscheinungsjahr
2015
Link zum Volltext
Quelle
SpringerLink (Online service)
Beschreibungen/Notizen
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 significantly 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 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.