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Journal of Bacteriology, January 2005, p. 522-533, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.522-533.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Intimin-Mediated Export of Passenger Proteins Requires Maintenance of a Translocation-Competent Conformation

Thorsten M. Adams,{dagger} Alexander Wentzel,{dagger},{ddagger} and Harald Kolmar*

Abteilung für Molekulare Genetik und Präparative Molekularbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität Göttingen, Göttingen, Germany

Received 12 March 2004/ Accepted 5 October 2004

Intimins from pathogenic bacteria promote intimate bacterial adhesion to epithelial cells. Several structurally similar domains form on the bacterial cell surface an extended rigid rod that exposes the carboxy-terminal domain, which interacts with the translocated intimin receptor. We constructed a series of intimin-derived fusion proteins consisting of carboxy-terminally truncated intimin and the immunoglobulin light-chain variable domain REIv, ubiquitin, calmodulin, ß-lactamase inhibitor protein, or ß-lactamase. By systematically investigating the intimin-mediated cell surface exposure of these passenger domains in the presence or absence of compounds that interfere with outer membrane stability or passenger domain folding, we acquired experimental evidence that intimin-mediated protein export across the outer membrane requires, prior to export, the maintenance of a translocation-competent conformation that may be distinct from the final protein structure. We propose that, during export, competition exists between productive translocation and folding of the passenger domain in the periplasm into a stable conformation that is not compatible with translocation through the bacterial outer membrane. These results may expand understanding of the mechanism by which intimins are inserted into the outer membrane and expose extracellular domains on the cell surface.

* Corresponding author. Mailing address: Abteilung für Molekulare Genetik und Präparative Molekularbiologie, Grisebachstr. 8, D-37077 Göttingen, Germany. Phone: 49 551 39 9657. Fax: 49 551 39 3805. E-mail: HKolmar{at}Uni-MolGen.gwdg.de.

{dagger} T.M.A. and A.W. contributed equally to this work.

{ddagger} Present address: Selecore GmbH, Göttingen, Germany.

Journal of Bacteriology, January 2005, p. 522-533, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.522-533.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bodelon, G., Marin, E., Fernandez, L. A. (2009). Role of Periplasmic Chaperones and BamA (YaeT/Omp85) in Folding and Secretion of Intimin from Enteropathogenic Escherichia coli Strains. J. Bacteriol. 191: 5169-5179 [Abstract] [Full Text]  
  • Jose, J., Meyer, T. F. (2007). The Autodisplay Story, from Discovery to Biotechnical and Biomedical Applications. Microbiol. Mol. Biol. Rev. 71: 600-619 [Abstract] [Full Text]  


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