Related Experiment Video
Updated: Jul 15, 2025
Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Deglycosylation of eukaryotic-expressed flagellin restores adjuvanticity
Koemchhoy Khim1,2,3,4, Sao Puth1,3, Kamalakannan Radhakrishnan1,2
1Clinical Vaccine R&D Center, Chonnam National University, Hwasun-gun, Jeonnam, Republic of Korea.
Abstract:
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.
