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<i>In silico</i> design of a multiepitope subunit vaccine targeting <i>Salmonella enterica</i> serovar Infantis: an immunoinformatics and reverse vaccinology approach. [PDF]
Chundru D, Ghanem M.
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A gut sense for a microbial pattern regulates feeding. [PDF]
Liu WW +23 more
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Developing an innovative chimeric multi-epitope subunit vaccine against <i>Staphylococcus intermedius</i> using an immunoinformatics strategy via Multi-omics approaches. [PDF]
Naveed M +11 more
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Helicobacter pylori flagellin: TLR5 evasion and fusion-based conversion into a TLR5 agonist
Biochemical and Biophysical Research Communications, 2018Helicobacter pylori is a flagellated bacterium of the Epsilonproteobacteria class that causes peptic ulcers. Flagellin is a primary structural protein that assembles into the flagellar filament. Flagellins from bacteria that belong to the Gammaproteobacteria and Firmicutes groups are detected by Toll-like receptor 5 (TLR5) in the host, triggering the ...
Sung-Il Yoon +2 more
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Trends in Microbiology, 2001
The human gastrointestinal tract is a dynamic melting pot of commensal bacteria. Although the apical surface of intestinal epithelial cells lining the gut is constantly exposed to proinflammatory bacterial products, this rarely results in an inflammatory response.
Mark Slifka, James D Brien
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The human gastrointestinal tract is a dynamic melting pot of commensal bacteria. Although the apical surface of intestinal epithelial cells lining the gut is constantly exposed to proinflammatory bacterial products, this rarely results in an inflammatory response.
Mark Slifka, James D Brien
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Science Signaling, 2001
Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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Hayashi et al. characterized the transmembrane Toll-like receptor (TLR) 5 protein and identified a physiologically relevant ligand capable of activating TLR5 signaling. Overexpression of chimeric proteins consisting of the intracellular domain of TLR5 fused to the extracellular domain of CD4 (to promote dimerization)
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Activation of TLR5 induces podocyte apoptosis
Cell Biochemistry and Function, 2016The apoptosis plays a critical role in a number of inflammatory disorders. Bacterial infection is one of the causes inducing apoptosis. This study aims to investigate the mechanism by which activation of TLR5 induces podocyte apoptosis. In this study, a podocyte cell line was cultured in RPMI1640 medium. The expression of TLR5 was assessed by real‐time
Xu, Lin +7 more
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The flagellin-TLR5 axis: Therapeutic opportunities
Drug News & Perspectives, 2002Motile bacteria synthesize large-sized surface structures known as flagella through the ordered polymerization of protein subunits. Flagellin, a protein of 40-60 kDa, is the principal constituent of the flagellum; each flagellum consists of approximately 20,000 flagellin molecules.
Liaudet, L. +6 more
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TLR5 takes aim at bacterial propeller
Nature Immunology, 2003The Toll-like receptor (TLR) family targets pathogen-derived molecules in regions unlikely to change under selection pressures. For TLR5, which recognizes the protein flagellin, the function of the targeting motif is key.
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