The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine

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Abstract:

The F17-G adhesin at the tip of flexible F17 fimbriae of enterotoxigenic Escherichia coli mediates binding to N-acetyl-beta-D-glucosamine-presenting receptors on the microvilli of the intestinal epithelium of ruminants. We report the 1.7 A resolution crystal structure of the lectin domain of F17-G, both free and in complex with N-acetylglucosamine. The monosaccharide is bound on the side of the ellipsoid-shaped protein in a conserved site around which all natural variations of F17-G are clustered. A model is proposed for the interaction between F17-fimbriated E. coli and microvilli with enhanced affinity compared with the binding constant we determined for F17-G binding to N-acetylglucosamine (0.85 mM-1). Unexpectedly, the F17-G structure reveals that the lectin domains of the F17-G, PapGII and FimH fimbrial adhesins all share the immunoglobulin-like fold of the structural components (pilins) of their fimbriae, despite lack of any sequence identity. Fold comparisons with pilin and chaperone structures of the chaperone/usher pathway highlight the central role of the C-terminal beta-strand G of the immunoglobulin-like fold and provides new insights into pilus assembly, function and adhesion

Notes:

DA - 20030716 IS - 0950-382X (Print) LA - eng PT - Comparative Study PT - Journal Article RN - 0 (Adhesins, Bacterial) RN - 0 (Adhesins, Escherichia coli) RN - 0 (Escherichia coli Proteins) RN - 0 (F17-G protein, E coli) RN - 0 (Lectins) RN - 0 (PapG protein, E coli) RN - 0 (fimH protein, E coli) RN - 147680-16-8 (Fimbriae Proteins) RN - 7512-17-6 (Acetylglucosamine) SB - IM