Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: cystic fibrosis (CF) [ICD11:
CA25 
]
The structure was elucidated in this paperNCBI PubMed ID: 24841205Publication DOI: 10.1074/jbc.M114.562603Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.valvano
qub.ac.uk
Institutions: From the Centre for Infection and Immunity, School of Medicine, Dentistry and Biomedical Sciences, Queen's University, Belfast BT9 7AE, Ireland, United Kingdom, the Department of Microbiology and Immunology, University of Western Ontario, London, Ontario N6A 5C1, Canada
Burkholderia cenocepacia is an opportunistic pathogen threatening patients with cystic fibrosis. Flagella are required for biofilm formation, as well as adhesion to and invasion of epithelial cells. Recognition of flagellin via the Toll-like receptor 5 (TLR5) contributes to exacerbate B. cenocepacia-induced lung epithelial inflammatory responses. In this study, we report that B. cenocepacia flagellin is glycosylated on at least ten different sites with a single sugar, 4,6-dideoxy-4-(3-hydroxybutanoylamino)-D-glucose [D-Qui4N(3HOBut)]. We have identified key genes that are required for flagellin glycosylation including a predicted glycosyltransferase gene that is linked to the flagellin biosynthesis cluster, and a putative acetyltransferase gene located within the O-antigen lipopolysaccharide cluster. Another O-antigen cluster gene, rmlB, which is required for flagellin glycan and O-antigen biosynthesis, was essential for bacterial viability, uncovering a novel target against Burkholderia infections. Using glycosylated and non-glycosylated purified flagellin and a cell reporter system to assess TLR5-mediated responses, we also show that the presence of glycan in flagellin significantly impair the inflammatory response of epithelial cells. We therefore suggest that flagellin glycosylation reduces recognition of flagellin by host TLR5, providing an evasive strategy to infecting bacteria.
glycosylation, immune response, opportunistic pathogen, Flagellin, Burkholderia cenocepacia
Structure type: monomer
Location inside paper: p.19237, fig.3
Aglycon: flagellin
Trivial name: glycosylated flagellin
Methods: GC-MS, SDS-PAGE, DNA techniques, GC, Western blotting, biological assays, methanolysis, genetic methods, enzymatic digestion, LC-MS/MS
NCBI Taxonomy refs (TaxIDs): 95486
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error