Sammanfattning

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.

Nyckelord

fimbrial adhesions; Gram-negative pathogens; chaperone; usher machinery; mono- and polyadhesive binding; immunomodulatory activity; vaccines

Publicerad i

FEMS Microbiology Reviews
2010, Volym: 34, nummer: 3, sidor: 317-378
Utgivare: WILEY-BLACKWELL PUBLISHING, INC

SLU författare

• Zavialov, Anton

  • Institutionen för molekylärbiologi, Sveriges lantbruksuniversitet
    

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UKÄ forskningsämne

Mikrobiologi
Biokemi och molekylärbiologi


Publikationens identifierare

DOI: https://doi.org/10.1111/j.1574-6976.2009.00201.x

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/43072