Adhesive organelles of Gram-negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint.
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 γ3- and κ-monophyletic groups, respectively, while gene clusters belonging to the γ1-, γ2-, γ4-, and π-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.
Zav'yalov
Vladimir
V
Joint Biotechnology Laboratory, University of Turku, Turku, Finland. vlazav@utu.fi
Zavialov
Anton
A
Zav'yalova
Galina
G
Korpela
Timo
T
D001422:Bacterial Adhesion; D036781:Fimbriae Proteins / Q000378:metabolism* / Q000648:ultrastructure; D010861:Fimbriae, Bacterial / Q000378:metabolism* / Q000648:ultrastructure; D006090:Gram-Negative Bacteria / Q000472:pathogenicity* / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D046911:Macromolecular Substances / Q000378:metabolism / Q000648:ultrastructure; D026901:Membrane Transport Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism; D055503:Protein Multimerization; D021381:Protein Transport
D046911:Macromolecular Substances; D026901:Membrane Transport Proteins; D018832:Molecular Chaperones; D036781:Fimbriae Proteins