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|Title:||Comparative virulence of Streptococcus pneumoniae strains with insertion-duplication, point, and deletion mutations in the pneumolysin gene|
|Citation:||Infection and Immunity, 1999; 67(2):981-985|
|Publisher:||American Society for Microbiology|
|Anne M. Berry, A. David Ogunniyi, David C. Miller and James C. Paton|
|Abstract:||Pneumolysin is a 471-amino-acid toxin produced byStreptococcus pneumoniae which has both cytolytic and complement activation properties. We have constructed a derivative of the type 2 S. pneumoniae strain D39 in which the portion of the pneumolysin gene encoding amino acids 55 to 437 has been deleted in-frame. The virulence of this strain (ΔPly) was compared with those of wild-type D39, a pneumolysin insertion-duplication mutant (PLN-A), and a derivative (PdT) carrying a toxin gene with three point mutations known to abolish both cytolytic activity and complement activation. PdT was intermediate in virulence between D39 and either PLN-A or ΔPly in a mouse intraperitoneal challenge model. This provides unequivocal evidence that pneumolysin has an additional property that is not abolished by point mutations which reduce cytotoxicity and complement activation to virtually undetectable levels.|
Mice, Inbred BALB C
|Rights:||© 1999, American Society for Microbiology|
|Appears in Collections:||Aurora harvest 2|
Molecular and Biomedical Science publications
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