Glycerol-induced unraveling of the tight helical conformation of Escherichia coli type 1 fimbriae
| Autor: | Soman N. Abraham, D. L. Hasty, R. Endres, M. Land, Jegdish Babu, S. Ponniah |
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| Rok vydání: | 1992 |
| Předmět: |
Glycerol
animal structures Protein Conformation Fimbria Biology medicine.disease_cause Microbiology Pilus Epitope Protein structure Escherichia coli medicine Trypsin Molecular Biology Depolymerization biochemical phenomena metabolism and nutrition bacterial infections and mycoses biology.organism_classification Enterobacteriaceae female genital diseases and pregnancy complications Biochemistry Fimbriae Bacterial bacteria Research Article medicine.drug |
| Zdroj: | Journal of Bacteriology. 174:5145-5148 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.174.15.5145-5148.1992 |
| Popis: | Glycerol was found to unravel the helical conformation of Escherichia coli type 1 fimbriae without appreciable depolymerization. The linearized fimbrial polymers have a diameter of 2 nm, react strongly with a monoclonal antibody directed at an inaccessible epitope on native fimbriae, and display greater mannose-binding activity and trypsin sensitivity than native fimbriae. Removal of glycerol by dialysis results in spontaneous reassembly of the linear polymers into structures morphologically, antigenically, and functionally indistinguishable from native fimbriae. |
| Databáze: | OpenAIRE |
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