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Research Article

Membrane Targeting of a Bacterial Virulence Factor Harbouring an Extended Signal Peptide

Chevalier N.a · Moser M.a · Koch H.-G.a · Schimz K.-L.b · Willery E.c · Locht C.c · Jacob-Dubuisson F.c,1 · Müller M.a,1

Author affiliations

aInstitut für Biochemie and Molekularbiologie, Universität Freiburg, Freiburg, and bInstitut für Biotechnologie, Forschungszentrum Jülich, Jülich, Germany; cINSERM U447, Institut de Biologie de Lille, Institut Pasteur de Lille, Lille, France

Related Articles for ""

J Mol Microbiol Biotechnol 2004;8:7–18

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Article / Publication Details

First-Page Preview
Abstract of Research Article

Published online: February 11, 2005
Issue release date: February 2005

Number of Print Pages: 12
Number of Figures: 8
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

Abstract

Filamentous haemagglutinin (FHA) is the major adhesin of Bordetella pertussis, the whooping cough agent. FHA is synthesized as a 367-kDa precursor harbouring a remarkably long signal peptide with an N-terminal extension that is conserved among related virulence proteins. FHA is secreted via the two-partner secretion pathway that involves transport across the outer membrane by a cognate transporter protein. Here we have analyzed the mechanism by which FHA is targeted to, and translocated across, the inner membrane. Studies were performed both in vitro using Escherichia coli inside-out inner membrane vesicles and in vivo by pulse-chase labelling of Bordetella pertussis cells. The data collectively indicate that like classical periplasmic and outer membrane proteins, FHA requires SecA and SecB for its export through the SecYEG translocon in the inner membrane. Although short nascent chains of FHA were found to cross-link to signal recognition particle (SRP), we did not obtain indication for an SRP-dependent, co-translational membrane targeting provoked by the FHA signal sequence. Our results rule out that the extended signal peptide of FHA determines a specific mode of membrane targeting but rather suggest that it might influence the export rate at the inner membrane.

© 2004 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Research Article

Published online: February 11, 2005
Issue release date: February 2005

Number of Print Pages: 12
Number of Figures: 8
Number of Tables: 0

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB


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