This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Burns, D. L. Articles by Verma, A. Search for Related Content PubMed PubMed Citation Articles by Burns, D. L. Articles by Verma, A.

 Previous Article  |  Next Article 

Infection and Immunity, September 2004, p. 5365-5372, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5365-5372.2004

Analysis of Subassemblies of Pertussis Toxin Subunits In Vivo and Their Interaction with the Ptl Transport Apparatus

Drusilla L. Burns,^* Stefanie Fiddner, Anissa M. Cheung, and Anita Verma

Laboratory of Respiratory and Special Pathogens, Food and Drug Administration, Bethesda, Maryland

Received 9 April 2004/ Returned for modification 10 May 2004/ Accepted 3 June 2004

Pertussis toxin (PT) has an AB₅ structure that is typical of many bacterial protein toxins; however, this toxin is more complex than many toxins since it is composed of five different subunit types, subunits S1 to S5. Little is known about how PT assembles in vivo and how and when it interacts with its secretion apparatus, known as the Ptl transporter. In order to better understand these events, we expressed subsets of the genes encoding the S1, S2, and/or S4 subunits of PT in strains of Bordetella pertussis that either did or did not produce the Ptl proteins. We found evidence to suggest that certain subassemblies of the toxin, including subassemblies consisting of the S1 subunit and incomplete forms of the B oligomer, can form in vivo, at least transiently. These results suggest that the B oligomer of the toxin does not need to completely form before interactions between the S1 subunit and B-oligomer subunits can occur in vivo. All subassemblies localized primarily to the membrane fraction of the cell. Moreover, we found that Ptl-mediated secretion occurs in a strain that produces S1 and an incomplete complement of B-oligomer subunits. These results indicate that subassemblies of the toxin consisting of the S1 subunit and a partial B oligomer can interact with the Ptl system.

---

* Corresponding author. Mailing address: CBER, FDA HFM-434, Building 29, Room 130, 8800 Rockville Pike, Bethesda, MD 20892. Phone: (301) 402-3553. Fax: (301) 402-2776. E-mail: burns{at}cber.fda.gov.

Editor: J. T. Barbieri

---

Infection and Immunity, September 2004, p. 5365-5372, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.5365-5372.2004

This article has been cited by other articles:

• Verma, A., Burns, D. L. (2007). Requirements for Assembly of PtlH with the Pertussis Toxin Transporter Apparatus of Bordetella pertussis. Infect. Immun. 75: 2297-2306 [Abstract] [Full Text]  
• Mattoo, S., Cherry, J. D. (2005). Molecular Pathogenesis, Epidemiology, and Clinical Manifestations of Respiratory Infections Due to Bordetella pertussis and Other Bordetella Subspecies. Clin. Microbiol. Rev. 18: 326-382 [Abstract] [Full Text]