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PMID: 10858221 Published · ppublish English Journal Article

Importance of holotoxin assembly in Ptl-mediated secretion of pertussis toxin from Bordetella pertussis.

Infection and immunity ·Vol. 68 ·No. 7 ·2000-07-00 ·Pages 4049-54

Farizo KM, Huang T, Burns DL

Abstract

We examined the structural components of pertussis toxin that are required for efficient export from Bordetella pertussis via the Ptl system, a member of the type IV family of macromolecular transporters. First, we constructed a strain of B. pertussis that contains a functional Ptl system but does not produce pertussis toxin. Plasmids which express either the S1 subunit or the B oligomer were then introduced into this strain. We found that the B oligomer of the toxin is not secreted in the absence of the S1 subunit. Conversely, the S1 subunit is also not secreted by a Ptl-mediated mechanism in the absence of the B oligomer. Thus, an assembled holotoxin is required for Ptl-mediated export of pertussis toxin from B. pertussis.

MeSH Terms
Base Sequence Biological Transport, Active Bordetella pertussis/genetics,metabolism,pathogenicity DNA Primers/genetics Genes, Bacterial Pertussis Toxin Plasmids/genetics Protein Structure, Quaternary Sequence Deletion Virulence Virulence Factors, Bordetella/chemistry,genetics,metabolism
Chemicals
DNA Primers Virulence Factors, Bordetella Pertussis Toxin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Farizo K M
Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, USA. farizo@cber.fda.gov
Huang T
Burns D L
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
2000-07-00
Pages
4049-54
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC101693
Subset
IM
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