Related Experiment Video
Updated: Aug 9, 2026

Establishment and Characterization of UTI and CAUTI in a Mouse Model
Published on: June 23, 2015
Host-specificity of uropathogenic Escherichia coli depends on differences in binding specificity to Gal alpha
N Strömberg1, B I Marklund, B Lund
1Department of Cariology, Faculty of Odontology, University of Gothenburg, Sweden.
Abstract:
Four G adhesins, cloned from uropathogenic Escherichia coli strains, were examined for binding to glycolipids and various eukaryotic cells. PapGAD110 and PapGIA2 showed virtually identical binding patterns to Gal alpha 1-4Gal-containing glycolipids, while PapGJ96 differed slightly and PrsGJ96 markedly with respect to the effect of neighbouring groups on the binding. Their hemagglutination patterns confirmed the existence of three receptor-binding specificities. While the PapG adhesins bound to uroepithelial cells from man (T24) but not to those from the dog (MDCK II), the reverse was true of PrsG. These binding patterns were largely explained by the absence or presence of appropriate glycolipid isoreceptors, although the inability of the PapG adhesins to bind MDCK II cells was attributed to an inappropriate presentation of their receptor epitopes. The high prevalence of PrsG-like specificities observed among wild-type dog uropathogenic E. coli isolates, together with the determined isoreceptor composition of human and dog kidney target tissues, suggest variation in receptor specificity as a mechanism for shifting host specificity, and that this variation has evolved in response to the topography of the host cellular receptors. The receptor-binding half proposed for the predicted amino acid sequences of the four G adhesins and the corresponding adhesin of one of the dog E. coli isolates varied considerably among the three receptor-binding groups of adhesins, but only little within each group.
Insights
This study reveals how uropathogenic Escherichia coli adhesins bind to host cells. Variations in adhesin receptor specificity explain differences in binding to human and dog cells, suggesting a mechanism for host adaptation.
Area of Science:
- Microbiology
- Molecular Biology
- Urology
Background:
- Uropathogenic Escherichia coli (UPEC) utilizes adhesins to colonize the urinary tract.
- G adhesins are crucial virulence factors in UPEC, mediating bacterial attachment to host cells.
- Understanding adhesin-receptor interactions is key to deciphering host specificity and developing targeted therapies.
Purpose of the Study:
- To characterize the glycolipid and eukaryotic cell binding specificities of four G adhesins from UPEC.
- To investigate the role of receptor binding variations in UPEC host specificity (human vs. dog).
- To correlate adhesin binding patterns with the presence of specific glycolipid isoreceptors on host cells.
Main Methods:
- Cloning and expression of four G adhesin variants from UPEC.
- Binding assays using purified glycolipids and eukaryotic cell lines (human T24, canine MDCK II).
- Hemagglutination assays to confirm receptor-binding specificities.
- Analysis of predicted amino acid sequences for receptor-binding domains.
Main Results:
- PapG adhesins (PapGAD110, PapGIA2, PapGJ96) exhibited similar binding to Gal alpha 1-4Gal-containing glycolipids, while PrsG adhesin (PrsGJ96) showed distinct patterns.
- PapG adhesins bound human uroepithelial cells but not canine cells, whereas PrsG adhesins showed the opposite preference.
- Binding patterns correlated with the presence of specific glycolipid isoreceptors, with steric hindrance potentially affecting PapG binding to canine cells.
Conclusions:
- G adhesin receptor specificity varies, influencing binding to different host cell types.
- Differences in glycolipid isoreceptor composition and presentation on host cells contribute to UPEC host specificity.
- Adhesin variation is a key evolutionary mechanism for UPEC adaptation to different hosts, driven by host receptor topography.
More Related Videos
08:13Producing Gene Deletions in Escherichia coli by P1 Transduction with Excisable Antibiotic Resistance Cassettes
Published on: September 1, 2018
09:44Characterization of a Pathogenic Escherichia coli Strain Derived from Oreochromis spp. Farms Using Whole-Genome Sequencing
Published on: December 23, 2022
Related Concept Videos
Ligand Binding Sites
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Ligand Binding and Linkage
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Chemotaxis in E. coli
Microbiota of the Urogenital Tract
Bacterial Gastroenteritis