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Infection and Immunity, February 1999, p. 981-985, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Comparative Virulence of Streptococcus pneumoniae Strains with Insertion-Duplication, Point, and Deletion Mutations in the Pneumolysin Gene

Anne M. Berry, A. David Ogunniyi, David C. Miller, and James C. Paton*

Molecular Microbiology Unit, Women's and Children's Hospital, North Adelaide, S.A., 5006, Australia

Received 27 August 1998/Returned for modification 14 October 1998/Accepted 17 November 1998

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 (Delta Ply) 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 Delta Ply 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.

* Corresponding author. Mailing address: Molecular Microbiology Unit, Women's and Children's Hospital, North Adelaide, S.A., 5006, Australia. Phone: 61-8-8204 6302. Fax: 61-8-8204 6051. E-mail: patonj{at}wch.sa.gov.au.

Infection and Immunity, February 1999, p. 981-985, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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