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pubmed:abstractText |
FedF is the two-domain tip adhesin of F18 fimbriae from enterotoxigenic Escherichia coli. Bacterial adherence, mediated by the N-terminal receptor-binding domain of FedF to carbohydrate receptors on intestinal microvilli, causes diarrhoea and oedema disease in newly weaned piglets and induces the secretion of Shiga toxins. A truncate containing only the receptor-binding domain of FedF was found to be further cleaved at its N-terminus. Reconstruction of this N-terminal truncate rendered FedF amenable to crystallization, resulting in crystals with space group P2(1)2(1)2(1) and unit-cell parameters a = 36.20, b = 74.64, c = 99.03 A that diffracted to beyond 2 A resolution. The binding specificity of FedF was screened for on a glycan array, exposing 264 glycoconjugates, to identify specific receptors for cocrystallization with FedF.
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pubmed:affiliation |
Department of Ultrastructure, Vrije Universiteit Brussel, Flanders Interuniversity Institute for Biotechnology, Pleinlaan 2, 1050 Brussels, Belgium.
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