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Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG.

par Van Molle, Inge;Moonens, Kristof;Garcia-Pino, Abel ;Buts, Lieven;De Kerpel, Maia;Wyns, Lode;Bouckaert, Julie;De Greve, Henri
Référence Journal of Molecular Biology, 394, 5, page (957-967)
Publication Publié, 2009-12

Article révisé par les pairs

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Résumé :

Enterotoxigenic Escherichia coli expressing F4 fimbriae are the major cause of porcine colibacillosis and are responsible for significant death and morbidity in neonatal and postweaned piglets. Via the chaperone-usher pathway, F4 fimbriae are assembled into thin, flexible polymers mainly composed of the single-domain adhesin FaeG. The F4 fimbrial system has been labeled eccentric because the F4 pilins show some features distinct from the features of pilins of other chaperone-usher-assembled structures. In particular, FaeG is much larger than other pilins (27 versus approximately 17 kDa), grafting an additional carbohydrate binding domain on the common immunoglobulin-like core. Structural data of FaeG during different stages of the F4 fimbrial biogenesis process, combined with differential scanning calorimetry measurements, confirm the general principles of the donor strand complementation/exchange mechanisms taking place during pilus biogenesis via the chaperone-usher pathway.