Toll-like receptor 5 recognizes a conserved site on flagellin required for protofilament formation and bacterial motility

By Kelly D. Smith, E. Andersen-Nissen, F. Hayashi, Katie L Strobe, M. Bergman, S. L. R. Barrett, B. Cookson, Alan Aderem. Nature Immunology, 2003

863 citations recorded by the source corpus.

Subfields: Endocrinology, Immunology, Pulmonary and Respiratory Medicine

View Paper: https://www.semanticscholar.org/paper/1e6b99fd9e7a752df2fb1b627889b11e2e2fb2ff

How researchers see this paper

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In Endocrinology

1. G. Núñez
2. S. Ghosh
3. N. Inohara

In Immunology

1. T. Kanneganti
2. S. Ghosh
3. G. Núñez
4. M. Hayden
5. A. West
6. L. Franchi
7. N. Inohara
8. T. Boller

In Pulmonary and Respiratory Medicine

1. Peter Vandenabeele

Citations in the corpus

• The N Terminus of Bacterial Elongation Factor Tu Elicits Innate Immunity in Arabidopsis Plants (2004, background): “Interestingly, TLR5 receptor of animal innate immunity also recognizes an epitope of flagellin that faces the inside of the intact flagellum (Smith et al., 2003), and other PAMPs stimulating the innate immune response in animals include cytoplasmic components such as the heat shock protein HSP60…”
• Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses (2004, background): “fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=7100">TLR5 , which binds to bacterial flagellin and activates host inflammatory response”
• Innate Immune Pattern Recognition: A Cell Biological Perspective (2015, neutral): “TLR5 recognizes flagellin (114, 115), a major antigenic target of flagellated gram-negative and gram-positive bacteria.”
• NF-κB and the immune response (2006, background): “Interestingly, the TLR5 recognition site is masked in the filamentous flagellar structure, thus indicating that TLR5 recognizes only monomeric flagellin (Smith et al., 2003).”
• The Structural Biology of Toll-Like Receptors (2011, background): “This domain is exposed in monomeric flagellin, but is buried in the polymerized flagellin fiber, suggesting that TLR5 recognizes flagellin monomers that are released upon depolymerization of flagellin polymers (Smith et al., 2003).”
• Comprehending crystalline β-carotene accumulation by comparing engineered cell models and the natural carotenoid-rich system of citrus (2011, neutral): “Additionally, even though the exposed domain of flagellin is highly variable (from almost absent up to 1000 amino acid residues), the flagellin protein is highly conserved in the non-exposed domain of the protein (Felix et al., 1999; Smith et al., 2003; Bardoel and Van Strijp, 2011).”
• Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. (2006, background): “Mammalian TLR5 influences host susceptibility to infection through recognition of the bacterial flagellin protein, the main subunit building the flagellar structure (Smith et al. 2003).”
• LPS, TLR4 and infectious disease diversity (2005, background): “The interaction between flagella and TLR5 could be important in this regar”
• How do plants achieve immunity? Defence without specialized immune cells (2012, background): “Although both receptors recognize conserved epitopes of bacterial flagellin, they bind to different epitopes within this MAM”
• Cytosolic flagellin requires Ipaf for activation of caspase-1 and interleukin 1β in salmonella-infected macrophages (2006, background): “Because we found FliC was essential for salmonella-induced IL-1β secretion, we tested whether substitution of a highly conserved isoleucine residue of FliC with alanine (I411A), which abolishes bacterial motilit”