Zavialov, Anton
- Department of Molecular Biology, Swedish University of Agricultural Sciences
Abstract
This review summarizes the current knowledge on the structure, function, assembly, and biomedical applications of the family of adhesive fimbrial organelles assembled on the surface of Gram-negative pathogens via the FGL chaperone/usher pathway. Recent studies revealed the unique structural and functional properties of these organelles, distinguishing them from a related family, FGS chaperone-assembled adhesive pili. The FGL chaperone-assembled organelles consist of linear polymers of one or two types of protein subunits, each possessing one or two independent adhesive sites specific to different host cell receptors. This structural organization enables these fimbrial organelles to function as polyadhesins. Fimbrial polyadhesins may ensure polyvalent fastening of bacteria to the host cells, aggregating their receptors and triggering subversive signals that allow pathogens to evade immune defense. The FGL chaperone-assembled fimbrial polyadhesins are attractive targets for vaccine and drug design.
Keywords
fimbrial polyadhesins; FGL chaperones; Gram-negative pathogens; anti-immune action; binding sites; B and T-cell epitopes; vaccines
Published in
FEMS Microbiology Reviews
2007, volume: 31, number: 4, pages: 478-514
Publisher: BLACKWELL PUBLISHING
SLU Authors
UKÄ Subject classification
Food Science
Publication identifier
- DOI: https://doi.org/10.1111/j.1574-6976.2007.00075.x
Permanent link to this page (URI)
https://res.slu.se/id/publ/22773