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Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains

Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia... Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains Esteban Veiga , Víctor de Lorenzo * , and Luis Angel Fernández Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus de Cantoblanco, 28049 Madrid, Spain ABSTRACT Hybrid proteins containing the β-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgAβ) and the partner leucine zippers of the eukaryotic transcriptional factors Fos and Jun were expressed in Escherichia coli. Such fusion proteins targeted the leucine zipper modules to the cell surface. Cells displaying the Junβ sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fosβ and Junβ chimeras formed stable bacterial consortia. These associations were physically held by tight intercell ties caused by the protein-protein interactions of matching dimerization domains. The role of autotransporters in the emergence of new adhesins is discussed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Bacteriology American Society For Microbiology

Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains

Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains

Journal of Bacteriology , Volume 185 (18): 5585 – Sep 15, 2003

Abstract

Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains Esteban Veiga , Víctor de Lorenzo * , and Luis Angel Fernández Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus de Cantoblanco, 28049 Madrid, Spain ABSTRACT Hybrid proteins containing the β-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgAβ) and the partner leucine zippers of the eukaryotic transcriptional factors Fos and Jun were expressed in Escherichia coli. Such fusion proteins targeted the leucine zipper modules to the cell surface. Cells displaying the Junβ sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fosβ and Junβ chimeras formed stable bacterial consortia. These associations were physically held by tight intercell ties caused by the protein-protein interactions of matching dimerization domains. The role of autotransporters in the emergence of new adhesins is discussed.

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References (51)

Publisher
American Society For Microbiology
Copyright
Copyright © 2003 by the American society for Microbiology.
ISSN
0021-9193
eISSN
1098-5530
DOI
10.1128/JB.185.18.5585-5590.2003
Publisher site
See Article on Publisher Site

Abstract

Autotransporters as Scaffolds for Novel Bacterial Adhesins: Surface Properties of Escherichia coli Cells Displaying Jun/Fos Dimerization Domains Esteban Veiga , Víctor de Lorenzo * , and Luis Angel Fernández Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus de Cantoblanco, 28049 Madrid, Spain ABSTRACT Hybrid proteins containing the β-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgAβ) and the partner leucine zippers of the eukaryotic transcriptional factors Fos and Jun were expressed in Escherichia coli. Such fusion proteins targeted the leucine zipper modules to the cell surface. Cells displaying the Junβ sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fosβ and Junβ chimeras formed stable bacterial consortia. These associations were physically held by tight intercell ties caused by the protein-protein interactions of matching dimerization domains. The role of autotransporters in the emergence of new adhesins is discussed.

Journal

Journal of BacteriologyAmerican Society For Microbiology

Published: Sep 15, 2003

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