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Infection and Immunity, March 2000, p. 1276-1281, Vol. 68, No. 3
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mutations in the S1 Subunit of Pertussis Toxin That Affect Secretion

Kathleen A. Craig-Mylius,dagger Trevor H. Stenson, and Alison A. Weiss*

Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati, Cincinnati, Ohio 45267-0524

Received 20 September 1999/Returned for modification 4 November 1999/Accepted 3 December 1999

Pertussis toxin is a member of the AB5 family of toxins and is composed of five subunits (S1 to S5) present in a 1:1:1:2:1 ratio. Secretion is a complex process. Each subunit has a secretion signal that mediates transport to the periplasm, where processing and assembly occur. Secretion of the assembled 105-kDa toxin past the outer membrane is mediated by the nine proteins encoded in the ptl operon. Previous studies have shown that S1, the catalytically active A subunit of pertussis toxin, is necessary for efficient secretion, suggesting that a domain on S1 may be required for interaction with the secretion apparatus. Previously, recombinant S1 from four different mutants (serine 54 to glycine, serine 55 to glycine, serine 56 to glycine, and arginine 57 to lysine) was shown to retain catalytic activity. We introduced these mutations into Bordetella pertussis and monitored pertussis toxin production and secretion. No pertussis toxin was detected in the serine 54-to-glycine mutant. The other S1 mutants produced periplasmic pertussis toxin, but little pertussis toxin secretion was observed. The arginine 57-to-lysine mutant had the most dramatic secretion defect. It produced wild-type levels of periplasmic pertussis toxin but secreted only 8% as much toxin as the wild-type strain. This phenotype was similar to that observed for strains with mutations in the ptl genes, suggesting that this region may have a role in pertussis toxin secretion.

* Corresponding author. Mailing address: Department of Molecular Genetics, Biochemistry, and Microbiology, 231 Bethesda Ave., ML 524, University of Cincinnati, Cincinnati, OH 45267. Phone: (513) 558-2820. Fax: (513) 558-8474. E-mail: alison.weiss{at}uc.edu.

dagger Present address: Department of Medicine, Division of Rheumatology/Immunology, New England Medical Center and Tufts University School of Medicine, Boston, MA 02111.

Infection and Immunity, March 2000, p. 1276-1281, Vol. 68, No. 3
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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