Phosphatidylethanolamine recognition promotes enteropathogenic E. coli and enterohemorrhagic E. coli host cell attachment
| Autor: | Debora Barnett Foster, Mario Huesca, Clifford A. Lingwood, Philip M. Sherman, Dana J. Philpott, Maan Abul-Milh |
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| Rok vydání: | 1999 |
| Předmět: |
Enzyme-Linked Immunosorbent Assay
Biology Escherichia coli O157 medicine.disease_cause Microbiology Bacterial Adhesion Pilus Cell Line chemistry.chemical_compound Glycolipid Cell surface receptor Escherichia coli medicine Humans Escherichia coli Infections Phospholipids Phosphatidylethanolamine Liposome Virulence Phosphatidylethanolamines Vesicle Phosphatidylserine biochemical phenomena metabolism and nutrition Infectious Diseases chemistry Liposomes bacteria lipids (amino acids peptides and proteins) Chromatography Thin Layer Glycolipids |
| Zdroj: | Microbial Pathogenesis. 27:289-301 |
| ISSN: | 0882-4010 |
| DOI: | 10.1006/mpat.1999.0305 |
| Popis: | Using both solid phase and liposome aggregation assays, we screened a variety of glycolipids and phospholipids and found that EHEC and EPEC bind specifically and in a dose-dependent manner to PE. This binding was consistently observed whether the lipid was immobilized on a thin layer chromatography plate, in a microtitre well or incorporated into a unilamellar vesicle suspended in aqueous solution. There was no evidence of binding to other phospholipids such as phosIphatidylcholine (PC) or phosphatidylserine (PS). Bacterial binding to two epithelial cell lines also correlated with the level of outer leaflet PE and was reduced following preincubation with anti-PE. The PE-binding phenotype of EPEC appeared to correlate with the bundle-forming pilus (bfp) genotype of a number of clinical isolates. These results provide evidence of a receptor role for PE in the adhesion of EHEC and EPEC to host cells. |
| Databáze: | OpenAIRE |
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