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Infection and Immunity, July 2000, p. 4049-4054, Vol. 68, No. 7
0019-9567/00/$04.00+0

Importance of Holotoxin Assembly in Ptl-Mediated Secretion of Pertussis Toxin from Bordetella pertussis

Karen M. Farizo,* Theresa Huang, and Drusilla L. Burns

Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892

Received 4 February 2000/Returned for modification 17 March 2000/Accepted 17 April 2000

We examined the structural components of pertussis toxin that are required for efficient export from Bordetella pertussis via the Ptl system, a member of the type IV family of macromolecular transporters. First, we constructed a strain of B. pertussis that contains a functional Ptl system but does not produce pertussis toxin. Plasmids which express either the S1 subunit or the B oligomer were then introduced into this strain. We found that the B oligomer of the toxin is not secreted in the absence of the S1 subunit. Conversely, the S1 subunit is also not secreted by a Ptl-mediated mechanism in the absence of the B oligomer. Thus, an assembled holotoxin is required for Ptl-mediated export of pertussis toxin from B. pertussis.

* Corresponding author. Mailing address: CBER, FDA HFM-434, Building 29, Room 418, 8800 Rockville Pike, Bethesda, MD 20892. Phone: (301) 496-2013. Fax: (301) 402-2776. E-mail: farizo{at}cber.fda.gov.

Infection and Immunity, July 2000, p. 4049-4054, Vol. 68, No. 7
0019-9567/00/$04.00+0


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