Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.345175
Title: The pathogenicity of Escherichia coli which cause diarrhoea in calves, with particular reference to the characterisation, distribution and role of adhesins
Author: Chanter, Neil
ISNI:       0000 0001 3528 5761
Awarding Body: University of Surrey
Current Institution: University of Surrey
Date of Award: 1983
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Abstract:
The K99 and anionic antigens of the K99 reference strain Escherichia coli B41 were purified by immunoelectrophoresis. SDS-PAGE revealed K99 to be composed of polypeptide subunits with a molecular weight of 19,000. The anionic antigen was composed of polypeptide subunits with a molecular weight of 34,000. The subunits of K99 adhered to sheep erythrocytes at 4°C but eluted from them at 37°C. The subunits of the anionic antigen adhered at 4°C and 37°C but did not elute at 56°C. Two mannose resistant haemagglutinins with molecular weights greater than 20 x 10⁶ were partially purified from a K99⁻ variant of E. coli B41. One was identical to the anionic antigen, adhered to calf brush borders and did not have a regular fimbrial structure. The second was a polymer of two polypeptide subunits with molecular weights of 49,500 and 48,000; it was antigenically distinct from K99 and the anionic antigen, did not adhere to brush borders or isolated villi and had a fimbrial structure. An immunoperoxidase test indicated that the second haemagglutin in was produced in the ileum of a gnotobiotic calf infected with E. coli B41. Agglutination of sheep erythrocytes by the second haemagglutin in was inhibited by any of ten sugars. The receptor was present in glycolipid extracts of sheep erythrocytes. K99 was the only detectable adhesin on E. coli B117. This organism produced three polypeptides of similar molecular weight to the anionic antigen which did not adhere to brush borders or isolated villi. Results of an immunoradiometric assay suggested that the K99 of different strains was not identical.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.345175  DOI: Not available
Keywords: Microbiology
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