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

QC 20230602
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 Angstrom 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.

Bouckaert, J (författare)
De Genst, E (författare)
Loris, R (författare)
Oscarson, S (författare)
Lahmann, Martina,Docent i kemi,1963-Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden(Swepub:kth)u190mcjj (författare)
Messens, J (författare)
Brosens, E (författare)
Wyns, L (författare)
De Greve, H (författare)
Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden (creator_code:org_t)

Av författaren/redakt...: Buts, L; Bouckaert, J; De Genst, E; Loris, R; Oscarson, S; Lahmann, Martina ...; visa fler...; Messens, J; Brosens, E; Wyns, L; De Greve, H; visa färre...

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