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

Abstract:

: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.

journal_name

Infect Immun

journal_title

Infection and immunity

authors

Berry AM,Ogunniyi AD,Miller DC,Paton JC

doi

10.1128/IAI.67.2.981-985.1999

subject

Has Abstract

pub_date

1999-02-01 00:00:00

pages

981-5

issue

2

eissn

0019-9567

issn

1098-5522

journal_volume

67

pub_type

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