IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
IAI.00736-06v1
75/2/932    most recent
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 Google Scholar
Google Scholar
Right arrow Articles by Nowrouzian, F. L.
Right arrow Articles by Wold, A. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nowrouzian, F. L.
Right arrow Articles by Wold, A. E.

 Previous Article  |  Next Article 

Infection and Immunity, February 2007, p. 932-940, Vol. 75, No. 2
0019-9567/07/$08.00+0     doi:10.1128/IAI.00736-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Reduced Phase Switch Capacity and Functional Adhesin Expression of Type 1-Fimbriated Escherichia coli from Immunoglobulin A-Deficient Individuals{triangledown}

Forough L. Nowrouzian,1* Vanda Friman,2 Ingegerd Adlerberth,1 and Agnes E. Wold1

Department of Clinical Bacteriology,1 Department of Infectious Diseases, Göteborg University, Göteborg, Sweden2

Received 8 May 2006/ Returned for modification 12 September 2006/ Accepted 2 November 2006

The mannose-specific adhesin of type 1 fimbriae is the most common adhesin in Escherichia coli. One receptor for this adhesin is the carbohydrate chains of secretory immunoglobulin A (S-IgA), and intestinal E. coli from IgA-deficient individuals has a reduced capacity to adhere to mannose-containing receptors. Here, we investigated the expression of the mannose-specific adhesin and its capacity to switch to the fimbriated phenotype in colonic resident and transient E. coli strains isolated from control (n = 16) and IgA-deficient (n = 17) persons. Resident E. coli strains from IgA-deficient individuals displayed weaker mannose-specific adherence to colonic cells than resident strains from control individuals (21 versus 44 bacteria/cell, P = 0.0009) due to three mechanisms: a lower carriage rate of the fimH gene (90% versus 97%, not significant), more frequent failure to switch on the fim genes (30% versus 6%, P = 0.02), and the reduced adhesive potential of fimH+ isolates capable of phase switch (26 versus 46 bacteria/cell, P = 0.02). On the other hand, resident strains from IgA-deficient individuals displayed stronger mannose-resistant adherence than resident strains from control individuals (P = 0.04) and transient strains from IgA-deficient individuals (P = 0.01). The presence of S-IgA appears to favor the establishment of E. coli clones which readily express mannose-specific adhesins in the bowel microbiota.


* Corresponding author. Mailing address: Department of Clinical Bacteriology, Guldhedsgatan 10, S-413 46 Göteborg, Sweden. Phone: 46-31-3424887. Fax: 46-31-3424975. E-mail: forough.nowrouzian{at}microbio.gu.se.

{triangledown} Published ahead of print on 13 November 2006.

Editor: V. J. DiRita


Infection and Immunity, February 2007, p. 932-940, Vol. 75, No. 2
0019-9567/07/$08.00+0     doi:10.1128/IAI.00736-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.







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 © 2007 by the American Society for Microbiology. All rights reserved.