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The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces.

Van Molle I, Moonens K, Buts L, Garcia-Pino A, Panjikar S, Wyns L, De Greve H, Bouckaert J
Acta Crystallogr D Biol Crystallogr 65 411-20 (2009)
Related entries: 3f6i, 3f6l

Cited: 4 times
EuropePMC logo PMID: 19390146

Abstract

Many Gram-negative bacteria use the chaperone-usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces.

Reviews citing this publication (2)

  1. Animal Enterotoxigenic Escherichia coli. Dubreuil JD, Isaacson RE, Schifferli DM. EcoSal Plus 7 (2016)
  2. Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint. Zav'yalov V, Zavialov A, Zav'yalova G, Korpela T. FEMS Microbiol Rev 34 317-378 (2010)

Articles citing this publication (2)

  1. Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG. Van Molle I, Moonens K, Garcia-Pino A, Buts L, De Kerpel M, Wyns L, Bouckaert J, De Greve H. J Mol Biol 394 957-967 (2009)
  2. The Escherichia coli P and Type 1 Pilus Assembly Chaperones PapD and FimC Are Monomeric in Solution. Sarowar S, Hu OJ, Werneburg GT, Thanassi DG, Li H. J Bacteriol 198 2360-2369 (2016)


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