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Purification and chemical properties of flagellin
Archives of Biochemistry and Biophysics, 1959Abstract A study of flagella and flagellin from six bacterial species led to the following generalizations: Flagella consist of proteins that, after removal from the cell bodies by shaking, can be isolated in highly purified condition by fractional centrifugation, or a combination of centrifugation and fractional precipitation with ammonium sulfate ...
T, KOBAYASHI, J N, RINKER, H, KOFFLER
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Relatedness of the flagellins from methanogens
Archives of Microbiology, 1992Purified flagellar filaments isolated from six methanogens were composed of multiple flagellins. Two flagellins were present in Methanococcus deltae (Mr = 34,000 and 32,000), Methanoculleus marisnigri (Mr = 31,000 and 25,500) and Methanococcus jannaschii (Mr = 31,000 and 27,500), three in Methanothermus fervidus (Mr = 34,000, 25,000 and 24,000) and ...
M L, Kalmokoff, S F, Koval, K F, Jarrell
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Flagellin Signalling in Plant Immunity
2007Like all higher living organisms, plants are constantly exposed to microbes that either grow epiphytically on the organ surface, establish beneficial interactions in specific tissues, or infect host tissues as pathogens and cause disease. In order to infect, pathogens must attach to the plant surface and break physical barriers to enter the tissue ...
Chinchilla, D., Boller, T., Robatzek, S.
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Flagellin as an object for supramolecular engineering
"Protein Engineering, Design and Selection", 1990A model of tertiary and quaternary structure of E. coli flagellin is suggested. According to this model, the molecule consists of two independent parts. One of them is formed by the N- and C-terminal regions of the polypeptide chain and is responsible for polymerization properties.
O V, Fedorov, A V, Efimov
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Medical Microbiology and Immunology, 1985
Ten antisera raised in rabbits, against polymeric flagellins from ten different Salmonella serotypes were used to determine the relative cross-activities between salmonella flagellins in monomeric form. The results showed a high degree of cross-reactivity between the antisera (IgG antibodies) and all monomeric flagellins investigated.
G F, Ibrahim +3 more
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Ten antisera raised in rabbits, against polymeric flagellins from ten different Salmonella serotypes were used to determine the relative cross-activities between salmonella flagellins in monomeric form. The results showed a high degree of cross-reactivity between the antisera (IgG antibodies) and all monomeric flagellins investigated.
G F, Ibrahim +3 more
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Science's STKE, 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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Science's STKE, 2001
Immune responses to flagellin have been evolutionarily conserved between plants and animals. In Arabidopsis , FLS2, a leucine-rich repeat (LRR) domain containing serine-threonine transmembrane kinase binds bacterial flagellin and mediates signals, culminating in a defensive response. Gómez-Gómez et al.
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Immune responses to flagellin have been evolutionarily conserved between plants and animals. In Arabidopsis , FLS2, a leucine-rich repeat (LRR) domain containing serine-threonine transmembrane kinase binds bacterial flagellin and mediates signals, culminating in a defensive response. Gómez-Gómez et al.
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Molecular Microbiology, 2016
SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yukio, Furukawa +7 more
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SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yukio, Furukawa +7 more
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How bacteria overcome flagellin pattern recognition in plants
Current Opinion in Plant Biology, 2022Gail Preston +2 more
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