Journal
FEMS MICROBIOLOGY REVIEWS
Volume 34, Issue 3, Pages 317-378Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6976.2009.00201.x
Keywords
fimbrial adhesions; Gram-negative pathogens; chaperone; usher machinery; mono- and polyadhesive binding; immunomodulatory activity; vaccines
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Funding
- European Commission [235538]
- Academy of Finland [112900]
- FORMAS [221-2007-1057]
- Swedish Research Council [K2008-58X-20689-01-3]
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This review summarizes current knowledge on the structure, function, assembly and biomedical applications of the superfamily of adhesive fimbrial organelles exposed on the surface of Gram-negative pathogens with the classical chaperone/usher machinery. High-resolution three-dimensional (3D) structure studies of the minifibers assembling with the FGL (having a long F1-G1 loop) and FGS (having a short F1-G1 loop) chaperones show that they exploit the same principle of donor-strand complementation for polymerization of subunits. The 3D structure of adhesive subunits bound to host-cell receptors and the final architecture of adhesive fimbrial organelles reveal two functional families of the organelles, respectively, possessing polyadhesive and monoadhesive binding. The FGL and FGS chaperone-assembled polyadhesins are encoded exclusively by the gene clusters of the gamma 3- and kappa-monophyletic groups, respectively, while gene clusters belonging to the gamma 1-, gamma 2-, gamma 4-, and pi-fimbrial clades exclusively encode FGS chaperone-assembled monoadhesins. Novel approaches are suggested for a rational design of antimicrobials inhibiting the organelle assembly or inhibiting their binding to host-cell receptors. Vaccines are currently under development based on the recombinant subunits of adhesins.
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