Essential role of the consensus nucleotide-binding site of PtlH in secretion of pertussis toxin from Bordetella pertussis.
PtlH is a member of a specialized set of transport proteins that is essential for secretion of pertussis toxin (PT) from Bordetella pertussis. Previously, PtlH was shown to contain a consensus nucleotide-binding motif. Here, we demonstrate that introduction of plasmids containing mutant forms of ptlH, altered in the putative nucleotide-binding region, into a wild-type strain of B. pertussis resulted in inhibition of PT secretion. Thus, this region of PtlH appears to be essential for protein function. Moreover, the observed dominant negative phenotype suggests that PtlH either functions as a multimer or interacts with another component necessary for secretion of PT.
Kotob
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Laboratory of Pertussis, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, USA.
Burns
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D001426:Bacterial Proteins; D001665:Binding Sites; D001692:Biological Transport; D001886:Bordetella pertussis / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D016384:Consensus Sequence; D026901:Membrane Transport Proteins; D016297:Mutagenesis, Site-Directed; D009711:Nucleotides / Q000378:metabolism; D037342:Pertussis Toxin; D010566:Virulence Factors, Bordetella / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D026901:Membrane Transport Proteins; D009711:Nucleotides; C109410:PtlH protein, Bordetella pertussis; D010566:Virulence Factors, Bordetella; D037342:Pertussis Toxin