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Tissue interactions of Escherichia coli adhesins
Antonie van Leeuwenhoek, 1988The E. coli adhesions show a remarkable tissue tropism in the human urinary tract. This obviously relates to the known compartmentation of glycoconjugates in the kidney. To function as a virulence factor in human urinary tract infections, an adhesin must evidently recognize such receptors at uroepithelia that are not excreted in soluble form in urine ...
T K, Korhonen +8 more
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The Fimbrial Adhesins of Escherichia Coli
1987Publisher Summary This chapter reviews the current knowledge of E. coli adhesions and their receptors. The main emphasis is given on the genetic and physiological aspects of adhesin production, the primary structure of adhesion subunits, their adhesive properties, and the characterization of adhesion receptors.
F K, De Graaf, F R, Mooi
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Acta Biotechnologica, 1990
AbstractE. coli has got increasing importance as a causative agent of intestinal and extra‐intestinal diseases. In both these infections adhesion of the bacteria to mucous surface cells are initial events for coionization and development of infection. Adhesins are bacterial recognition proteins which specifically interact with carbohydrate moieties of ...
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AbstractE. coli has got increasing importance as a causative agent of intestinal and extra‐intestinal diseases. In both these infections adhesion of the bacteria to mucous surface cells are initial events for coionization and development of infection. Adhesins are bacterial recognition proteins which specifically interact with carbohydrate moieties of ...
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Characterisation of Escherichia coli fimbrial and autotransporter adhesins
2022Escherichia coli is a Gram-negative bacterium that exhibits extensive diversity, ranging from a harmless commensal to a pathogen capable of causing serious intestinal and extra-intestinal infections. One feature that drives differences between commensal and pathogenic strains is the capacity to adhere to and colonise surfaces and form biofilms.
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Fimbrial adhesins from extraintestinal Escherichia coli
Environmental Microbiology Reports, 2010Summary Extraintestinal pathogenic Escherichia coli (ExPEC) represent an important subclass of E. coli that cause a wide spectrum of diseases in human and animal hosts. Fimbriae are key virulence factors of ExPEC strains.
Klemm, Per +2 more
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Adhesins of Enteropathogenic Escherichia coli
EcoSal Plus, 2006Enteropathogenic Escherichia coli (EPEC) strains induce morphological changes in infected epithelial cells. The resulting attaching and effacing (A/E) lesion is characterized by intimate bacterial adherence to epithelial cells, with microvillus destruction, cytoskeletal rearrangement, and aggregation of host ...
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Adhesins of Diffusely Adherent and Enteroaggregative Escherichia coli
EcoSal Plus, 2005Epidemiological studies have implicated enteroaggregative Escherichia coli (EAEC) strains in acute and persistent diarrhea in children, in food-borne diarrhea outbreaks, and in traveler's diarrhea, and this group is recognized as an emerging pathotype of enteric disease. Diffusely adherent E. coli
Chantal, Le Bouguénec, James P, Nataro
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Nonfimbrial Adhesins of Escherichia Coli
1996Pathogenic Escherichia coli exhibit a variety of adhesins classified according to their morphology, antigenic structure or receptor specificity.
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Fimbrial Adhesins of Escherichia coli
Clinical Infectious Diseases, 1985Fimbriae are long, threadlike protein polymers found on the surface of many strains of Escherichia coli. The presence of fimbriae has been found to be significantly correlated with pathogenicity, and specific fimbriae confer on pathogenic strains the ability to adhere to and colonize various specific host epithelia.
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Characterization of a Galactose Specific Adhesin of Enteroaggregative Escherichia coli
Archives of Biochemistry and Biophysics, 2001A fimbrial adhesin was identified from an enteroaggregative Escherichia coli strain. The adhesin was purified to 740-fold by sequential chromatography on an affinity matrix and gel filtration column in the FPLC system. The homogeneity of the purified protein was established by analytical isoelectrofocussing (pI 7.25).
V, Grover +5 more
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