IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sherlock, O.
Right arrow Articles by Klemm, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sherlock, O.
Right arrow Articles by Klemm, P.

 Previous Article  |  Next Article 

Infection and Immunity, April 2005, p. 1954-1963, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.1954-1963.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The TibA Adhesin/Invasin from Enterotoxigenic Escherichia coli Is Self Recognizing and Induces Bacterial Aggregation and Biofilm Formation

Orla Sherlock, Rebecca Munk Vejborg, and Per Klemm*

Microbial Adhesion Group, Centre for Biomedical Microbiology, BioCentrum-DTU, Technical University of Denmark, Lyngby, Denmark

Received 15 September 2004/ Returned for modification 20 October 2004/ Accepted 22 November 2004

Escherichia coli strains are responsible for many cases of gastrointestinal disease and represent a serious health problem worldwide. An essential step in the pathogenesis of such strains involves recognition and attachment to host intestinal surfaces. TibA is a potent bacterial adhesin associated with a number of enterotoxigenic E. coli strains and mediates bacterial attachment to a variety of human cells; additionally, it promotes invasion of such cells. This adhesin is a surface-displayed autotransporter protein and belongs to the exclusive group of bacterial glycoproteins; only the glycosylated form confers binding to and invasion of mammalian cells. Here we characterized TibA and showed that it possesses self-association characteristics and can mediate autoaggregation of E. coli cells. We demonstrated that intercellular TibA-TibA interaction is responsible for bacterial autoaggregation. Also, TibA expression significantly enhances biofilm formation by E. coli on abiotic surfaces.


* Corresponding author. Mailing address: Centre for Biomedical Microbiology, BioCentrum-DTU, Bldg. 301, Technical University of Denmark, DK-2800 Lyngby, Denmark. Phone: 45 45 25 25 06. Fax: 45 45 93 28 09. E-mail: pkl{at}biocentrum.dtu.dk.

Editor: A. D. O'Brien


Infection and Immunity, April 2005, p. 1954-1963, Vol. 73, No. 4
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.4.1954-1963.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2005 by the American Society for Microbiology. All rights reserved.