Comparative virulence of Streptococcus pneumoniae strains with insertion-duplication, point, and deletion mutations in the pneumolysin gene

Pneumolysin is a 471-amino-acid toxin produced by Streptococcus 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 delet...

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Bibliographic Details
Published in:Infection and immunity 1999-02, Vol.67 (2), p.981-985
Main Authors: BERRY, A. M, OGUNNIYI, A. D, MILLER, D. C, PATON, J. C
Format: Article
Language:English
Subjects:
Animals
Bacterial Proteins
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Gene Deletion
Gene Duplication
Genes, Bacterial
Mice
Mice, Inbred BALB C
Microbiology
Molecular and Cellular Pathogenesis
Mutagenesis, Insertional
Mutation
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Pneumococcal Infections - microbiology
Pneumococcal Infections - pathology
Point Mutation
Streptococcus pneumoniae
Streptococcus pneumoniae - genetics
Streptococcus pneumoniae - pathogenicity
Streptolysins - genetics
Streptolysins - toxicity
Virulence
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Summary:Pneumolysin is a 471-amino-acid toxin produced by Streptococcus 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 (DeltaPly) 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 DeltaPly 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.
ISSN:0019-9567
1098-5522
DOI:10.1128/iai.67.2.981-985.1999