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Journal of Bacteriology, September 2003, p. 5585-5590, Vol. 185, No. 18
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.18.5585-5590.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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

Received 2 May 2003/ Accepted 19 June 2003

Hybrid proteins containing the ß-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgAß) 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 Junß sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fosß and Junß 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.

* Corresponding author. Mailing address: Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus de Cantoblanco, 28049 Madrid, Spain. Phone: 34 91 585 4536. Fax: 43 91 585 4506. E-mail: vdlorenzo{at}cnb.uam.es.

Journal of Bacteriology, September 2003, p. 5585-5590, Vol. 185, No. 18
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.18.5585-5590.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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