NDLI: Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion

Content Provider	PubMed Central
Author	Farizo, Karen M. Stefanie, Fiddner Cheung, Anissa M. Burns, Drusilla L.
Copyright Year	2002
Abstract	Pertussis toxin is secreted from Bordetella pertussis with the assistance of the Ptl transport system, a member of the type IV family of macromolecular transporters. The S1 subunit and the B oligomer combine to form the holotoxin prior to export from the bacterial cell, although the site of assembly is not known. To better understand the pathway of pertussis toxin assembly and secretion, we examined the subcellular location of the S1 subunit, expressed with or without the B oligomer and the Ptl proteins. In wild-type B. pertussis, the majority of the S1 subunit that remained cell associated localized to the bacterial membranes. In mutants of B. pertussis that do not express pertussis toxin and/or the Ptl proteins, full-length S1, expressed from a plasmid, partitioned almost entirely to the bacterial membranes. Several lines of evidence strongly suggest that the S1 subunit localizes to the outer membrane of B. pertussis. First, we found that membrane-bound full-length S1 was almost completely insoluble in Triton X-100. Second, recombinant S1 previously has been shown to localize to the outer membrane of Escherichia coli (J. T. Barbieri, M. Pizza, G. Cortina, and R. Rappuoli, Infect. Immun. 58:999-1003, 1990). Third, the S1 subunit possesses a distinctive amino acid motif at its carboxy terminus, including a terminal phenylalanine, which is highly conserved among bacterial outer membrane proteins. By using site-directed mutagenesis, we determined that the terminal phenylalanine is critical for stable expression of the S1 subunit. Our findings provide evidence that prior to assembly with the B oligomer and independent of the Ptl proteins, the S1 subunit localizes to the outer membrane of B. pertussis. Thus, outer membrane-bound S1 may serve as a nucleation site for assembly with the B oligomer and for interactions with the Ptl transport system.
Related Links	http://dx.doi.org/10.1128/iai.70.3.1193-1201.2002
Ending Page	1201
Page Count	9
Starting Page	1193
File Format	PDF
ISSN	00199567
e-ISSN	10985522
Journal	Infection and Immunity
Issue Number	3
Volume Number	70
Language	English
Publisher	American Society for Microbiology
Publisher Date	2002-03-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Immunology Microbiology Parasitology Infectious Diseases Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Parasitology Immunology Microbiology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Mutations in the S1 Subunit of Pertussis Toxin That Affect Secretion

Reduced Glutathione Is Required for Pertussis Toxin Secretion by Bordetella pertussis

DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis

Localization of the promoter for the ptl genes of Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin.

Recombinant Mycobacterium bovis BCG Expressing Pertussis Toxin Subunit S1 Induces Protection against an Intracerebral Challenge with Live Bordetella pertussis in Mice

Recombinant Mycobacterium bovis BCG Expressing Pertussis Toxin Subunit S1 Induces Protection against an Intracerebral Challenge with Live Bordetella pertussis in Mice

Intracellular localization of the dermonecrotic toxin of Bordetella pertussis.

Expression of a C Terminally Truncated Form of Pertussis Toxin S1 Subunit Effectively Induces Protection against Pertussis Toxin following DNA-Based Immunization

Mucosal Immunization with a Genetically Engineered Pertussis Toxin S1 Fragment-Cholera Toxin Subunit B Chimeric Protein

Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion

Similar Documents

Mutations in the S1 Subunit of Pertussis Toxin That Affect Secretion

Reduced Glutathione Is Required for Pertussis Toxin Secretion by Bordetella pertussis

DsbA and DsbC Are Required for Secretion of Pertussis Toxin by Bordetella pertussis

Localization of the promoter for the ptl genes of Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin.

Recombinant Mycobacterium bovis BCG Expressing Pertussis Toxin Subunit S1 Induces Protection against an Intracerebral Challenge with Live Bordetella pertussis in Mice

Recombinant Mycobacterium bovis BCG Expressing Pertussis Toxin Subunit S1 Induces Protection against an Intracerebral Challenge with Live Bordetella pertussis in Mice

Intracellular localization of the dermonecrotic toxin of Bordetella pertussis.

Expression of a C Terminally Truncated Form of Pertussis Toxin S1 Subunit Effectively Induces Protection against Pertussis Toxin following DNA-Based Immunization

Mucosal Immunization with a Genetically Engineered Pertussis Toxin S1 Fragment-Cholera Toxin Subunit B Chimeric Protein

Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion