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Updated: Jul 2, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance
Published on: January 3, 2012
Stabilization of the pertussis toxin secretion apparatus by the C terminus of PtlD
Anita Verma1, Anissa M Cheung, Drusilla L Burns
1Laboratory of Respiratory and Special Pathogens, Food and Drug Administration, CBER, FDA HFM-434, Building 29, Room 130, 8800 Rockville Pike, Bethesda, MD 20892, USA.
Abstract:
Pertussis toxin (PT) is secreted from Bordetella pertussis by a type IV secretion system, known as the Ptl transporter, that comprises nine different proteins, PtlA to PtlI. In this study, we found that PtlD is required for the stability of three Ptl proteins, PtlE, PtlF, and PtlH. A region limited to the C-terminal 72 amino acids of PtlD (amino acids 392 to 463) was sufficient for maintaining the stability of PtlE, PtlF, and PtlH, although this region was not sufficient to support secretion of the toxin. Further analysis demonstrated that a stretch of 10 amino acids at the C-terminal end of PtlD (amino acids 425 to 434) contributes to transporter stability.
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