Title | Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG. |
Publication Type | Journal Article |
Year of Publication | 2009 |
Authors | Van Molle, I., K. Moonens, A. Garcia-Pino, L. Buts, M. De Kerpel, L. Wyns, J. Bouckaert, and H. De Greve |
Journal | J Mol Biol |
Volume | 394 |
Issue | 5 |
Pagination | 957-67 |
Date Published | 2009 Dec 18 |
Type of Article | smm |
ISSN | 1089-8638 |
Keywords | Adhesins, Escherichia coli, Enterotoxigenic Escherichia coli, Kinetics, Models, Molecular, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits, Thermodynamics |
Abstract | 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. |
DOI | 10.1016/j.jmb.2009.09.059 |
Alternate Journal | J. Mol. Biol. |
PubMed ID | 19799915 |
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