Investigating outer domain redundancy of the bacterial flagellar filament (#254)
Jacob Scadden
1
,
Pietro Ridone
1
,
Divyangi Pandit
1
,
Yoshiyuki Sowa
2
3
,
Matt AB Baker
1
- University of New South Wales, Sydney, NSW, Australia
- Department of Frontier Bioscience, Hosei University, Tokyo, Japan
- Research Center for Micro-Nano Technology, Hosei University, Tokyo, Japan
Publish consent withheld
- Kang, X et al. “Amino acids 89-96 of Salmonella flagellin: a key site for its adjuvant effect independent of the TLR5 signaling pathway.” Cellular & molecular immunology vol. 14,12 (2017): 1023-1025.
- Biedma, ME et al. “Recombinant flagellins with deletions in domains D1, D2, and D3: Characterization as novel immunoadjuvants.” Vaccine vol. 37,4 (2019): 652-663.
- Kreutzberger, M.A.B., Sobe, R.C., Sauder, A.B. et al. Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments. Nat Commun 13, 1422 (2022)
- Wang, F. et al. A structural model of flagellar filament switching across multiple bacterial species. Nat. Commun. 8, 960 (2017).
- Scadden, J., et al. Rescue of bacterial motility using two and three-species FliC chimeras. bioRxiv 2024.12.02.626473 (Currently in review at Journal of Bacteriology).