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Journal of Bacteriology, November 2008, p. 7285-7290, Vol. 190, No. 21
0021-9193/08/$08.00+0 doi:10.1128/JB.01106-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Laboratory of Respiratory and Special Pathogens, Food and Drug Administration, Bethesda, Maryland 20892
Received 7 August 2008/ Accepted 18 August 2008
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.
Published ahead of print on 22 August 2008.
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