Open AccessStabilization of the Pertussis Toxin Secretion Apparatus by the C Terminus of PtlD
Author(s) -
Anita Verma,
Anissa M. Cheung,
Drusilla L Burns
Publication year - 2008
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.01106-08
Subject(s) - bordetella pertussis , biology , secretion , pertussis toxin , toxin , amino acid , transporter , biochemistry , microbiology and biotechnology , g protein , bacteria , gene , receptor , genetics
Pertussis toxin (PT) is secreted fromBordetella 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.