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- W4366384814 endingPage "101330" @default.
- W4366384814 startingPage "101330" @default.
- W4366384814 abstract "Flagellin is the cognate ligand for host pattern recognition receptors, toll-like receptor 5 (TLR5) in the cell surface, and NAIP5/NLRC4 inflammasome in the cytosol. TLR5-binding domain is located in D1 domain, where crucial amino acid sequences are conserved among diverse bacteria. The highly conserved C-terminal 35 amino acids of flagellin were proved to be responsible for the inflammasome activation by binding to NAIP5. D2/D3 domains, located in the central region and exposed to the outside surface of flagellar filament, are heterogeneous across bacterial species and highly immunogenic. Taking advantage of TLR5- and NLRC4-stimulating activities, flagellin has been actively developed as a vaccine adjuvant and immunotherapeutic. Because of its immunogenicity, there exist worries concerning diminished efficacy and possible reactogenicity after repeated administration. Deimmunization of flagellin derivatives while preserving the TLR5/NLRC4-mediated immunomodulatory activity should be the most reasonable option for clinical application. This review describes strategies and current achievements in flagellin deimmunization." @default.
- W4366384814 created "2023-04-21" @default.
- W4366384814 creator A5011767899 @default.
- W4366384814 creator A5020931102 @default.
- W4366384814 creator A5021717111 @default.
- W4366384814 creator A5048419154 @default.
- W4366384814 creator A5065839577 @default.
- W4366384814 date "2023-06-01" @default.
- W4366384814 modified "2023-09-27" @default.
- W4366384814 title "Deimmunization of flagellin adjuvant for clinical application" @default.
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