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. 2004 Dec;186(23):8058-65.
doi: 10.1128/JB.186.23.8058-8065.2004.

Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation

Orla Sherlock  1 , Mark A Schembri, Andreas Reisner, Per Klemm
Affiliations

Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation

Orla Sherlock et al. J Bacteriol. 2004 Dec.

Abstract

Diarrhea-causing Escherichia coli strains are responsible for numerous cases of gastrointestinal disease and constitute a serious health problem throughout the world. The ability to recognize and attach to host intestinal surfaces is an essential step in the pathogenesis of such strains. AIDA is a potent bacterial adhesin associated with some diarrheagenic E. coli strains. AIDA mediates bacterial attachment to a broad variety of human and other mammalian cells. It is a surface-displayed autotransporter protein and belongs to the selected group of bacterial glycoproteins; only the glycosylated form binds to mammalian cells. Here, we show that AIDA possesses self-association characteristics and can mediate autoaggregation of E. coli cells. We demonstrate that intercellular AIDA-AIDA interaction is responsible for bacterial autoaggregation. Interestingly, AIDA-expressing cells can interact with antigen 43 (Ag43)-expressing cells, which is indicative of an intercellular AIDA-Ag43 interaction. Additionally, AIDA expression dramatically enhances biofilm formation by E. coli on abiotic surfaces in flow chambers.

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Figures

FIG. 1.
FIG. 1.
(A) Overview of the plasmid constructs used for expression AIDA (pOS33) and glycosylated AIDA (pLH44). The constructs were made in the pACYC184 cloning vector and were constitutively expressed. (B) Coomassie brilliant blue-stained SDS-PAGE gel of AIDA (lane 1) and glycosylated AIDA (lane 2) α-subunit proteins liberated from E. coli MS427 host cells by brief heat treatment.
FIG. 2.
FIG. 2.
Cell-cell aggregation characteristics (left panels) and settling from static liquid suspensions (right panels) of E. coli MS427 containing either the vector control plasmid pACYC184 (A), the aah-aidA-encoding plasmid pLH44 (B), or the aidA-encoding plasmid pOS33 (C).
FIG. 3.
FIG. 3.
Autoaggregation assay demonstrating the settling profiles of liquid suspensions of E. coli strains OS70 (vector control), OS71 (AAH-AIDA+), OS101 (AAH+), OS85 (AIDA+), and OS68 (Ag43+).
FIG. 4.
FIG. 4.
Confocal scanning laser microscopy showing cell autoaggregation mediated by specific AIDA-AIDA interactions. (A) SAR19 (Cfp+) and SAR20 (Yfp+). (B) SAR19 (Cfp+) and OS46 (Yfp+ AAH-AIDA+). (C) OS45 (Cfp+ AAH-AIDA+) and OS46 (Yfp+ AAH-AIDA+).
FIG. 5.
FIG. 5.
Confocal scanning laser microscopy showing cell aggregation mediated by glycosylated AIDA-Ag43 and AIDA-Ag43 interactions. (A) MS427 (Gfp+) and MS427 (DsRed+). (B) MS427 (Gfp+ AAH-AIDA+) and MS427 (DsRed+). (C) MS427 (DsRed+ Ag43+) and MS427 (Gfp+). (D) MS427 (Gfp+ AAH-AIDA+) and MS427 (DsRed+ Ag43+). (E) MS427 (Gfp+ Ag43+) and MS427 (DsRed+ AIDA+).
FIG. 6.
FIG. 6.
AIDA-mediated cell aggregation is blocked by fimbriae. (A) Coomassie brilliant blue-stained SDS-PAGE gel of glycosylated AIDA α-subunit proteins liberated from E. coli MS427 and E. coli MS427 (Fim+) host cells, showing that overexpression of type 1 fimbriae does not affect surface presentation of AIDA. (B) Fimbria production prevents AIDA settling in static liquid suspensions.
FIG. 7.
FIG. 7.
Spatial distribution of biofilm formation for Gfp-labeled E. coli strains OS70 (vector control) (A), OS68 (Ag43+), (B), and OS71 (AAH-AIDA+) (C). Biofilm development was monitored by confocal scanning laser microscopy at 15 h (left panels) and 30 h (right panels) after inoculation. The images are representative horizontal sections collected within each biofilm and vertical sections (to the right and below of each larger panel, representing the yz plane and the xz plane, respectively) at the positions indicated by the white lines.
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References

    1. Bachmann, B. 1996. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12, p. 2460-2488. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, D.C.
    1. Benz, I., and M. A. Schmidt. 1989. Cloning and expression of an adhesin (AIDA) involved in diffuse adherence of enteropathogenic Escherichia coli. Infect. Immun. 57:1506-1511. - PMC - PubMed
    1. Benz, I., and M. A. Schmidt. 1992. Isolation and serologic characterization of AIDA, the adhesin mediating the diffuse adherence phenotype of the diarrhea-associated Escherichia coli strain 2787(O126:H27). Infect. Immun. 60:13-18. - PMC - PubMed
    1. Benz, I., and M. A. Schmidt. 1992. AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787(O126:H27), is synthesized via a precursor molecule. Mol. Microbiol. 6:1539-1546. - PubMed
    1. Benz, I., and M. A. Schmidt. 2001. Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA adhesin. Mol. Microbiol. 40:1403-1413. - PubMed

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