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 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 Hartland, E. L.
Right arrow Articles by Frankel, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hartland, E. L.
Right arrow Articles by Frankel, G.

Infection and Immunity, August 2000, p. 4637-4646, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Expression of Intimin gamma  from Enterohemorrhagic Escherichia coli in Citrobacter rodentium

Elizabeth L. Hartland,1 Veronika Huter,1,dagger Lisa M. Higgins,2 Nathalie S. Goncalves,2 Gordon Dougan,1 Alan D. Phillips,3 Thomas T. MacDonald,2 and Gad Frankel1,*

Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AZ,1 Department of Paediatric Gastroenterology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, St. Bartholomew's Hospital, London EC1A 7BE,2 and University Department of Paediatric Gastroenterology, Royal Free Hospital, London NW3 2QG,3 United Kingdom

Received 10 February 2000/Returned for modification 18 April 2000/Accepted 17 May 2000

The carboxy-terminal 280 amino acids (Int280) of the bacterial adhesion molecule intimin include the receptor-binding domain. At least five different types of Int280, designated alpha , beta , gamma , delta , and varepsilon , have been described based on sequence variation in this region. Importantly, the intimin types are associated with different evolutionary branches and contribute to distinct tissue tropism of intimin-positive bacterial pathogens. In this study we engineered a strain of Citrobacter rodentium, which normally displays intimin beta , to express intimin gamma  from enterohemorrhagic Escherichia coli. We show that intimin gamma  binds to the translocated intimin receptor (Tir) from C. rodentium and has the ability to produce attaching and effacing lesions on HEp-2 cells. However, C. rodentium expressing intimin gamma  could not colonize orally infected mice or induce mouse colonic hyperplasia. These results suggest that intimin may contribute to host specificity, possibly through its interaction with a receptor on the host cell surface.


* Corresponding author. Mailing address: Department of Biochemistry, Imperial College, London SW7 2AZ, United Kingdom. Phone: 44-20-7594-5253. Fax: 44-20-7594-5255. E-mail: g.frankel{at}ic.ac.uk.

dagger Present address: Institute of Microbiology and Genetics, University of Vienna, A-1030 Vienna, Austria.


Infection and Immunity, August 2000, p. 4637-4646, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, 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 © 2000 by the American Society for Microbiology. All rights reserved.