Journal
NPJ VACCINES
Volume 8, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41541-023-00738-3
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Enzymatic deglycosylation restores the TLR5 stimulating functionality of eukaryotic-expressed Vibrio vulnificus flagellin B (eFlaB), suggesting that glycosylation interferes with eFlaB binding to TLR5. Site-directed mutagenesis of N-glycosylation residues restores TLR5 stimulation and adjuvanticity.
Flagellin, the TLR5 agonist, shows potent adjuvant activities in diverse vaccines and immunotherapies. Vibrio vulnificus flagellin B expressed in eukaryotic cells (eFlaB) could not stimulate TLR5 signaling. Enzymatic deglycosylation restored eFlaB's TLR5 stimulating functionality, suggesting that glycosylation interferes with eFlaB binding to TLR5. Site-directed mutagenesis of N-glycosylation residues restored TLR5 stimulation and adjuvanticity. Collectively, deglycosylated eFlaB may provide a built-in adjuvant platform for eukaryotic-expressed antigens and nucleic acid vaccines.
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