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Flagellin protein

Wu JY, Newton S, Judd A, Stocker B, Robinson WS, Expression of immunogenic epitopes of hepatitis B surface antigen with hybrid flagellin proteins by a vaccine strain of Salmonella, Proc. Natl. Acad. Sci. USA, 86 4726 1730, 1989. [Pg.405]

Flagellin. Protein which is the primary component of prokaryotic flagella. [Pg.511]

Endogenous promoters B. hermsii flagellin protein (flaB-P) and flagellarrod protein iflgB-P). [Pg.70]

In our unpublished genome sequence database for B. hermsii, we identified DNA sequences of the promoter for the flagellar rod protein (flgB-P), the promoter for the flagellin protein (flaB-P), and the variable tick protein gene (vtp). Sequences... [Pg.76]

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. [Pg.211]

Hin recombinase FljB flagellin FljA protein (repressor) ... [Pg.1100]

Fig. 9. Coiled-coil spirals. For the phage coat proteins and flagellin, subunits are shown enlarged next to the structures, as well as the cross sections of the coiled-coil sheets they form. The positions of the subunits in the structures are indicated in white. The core packing layers are also shown for the phage coat proteins in order to illustrate the use of knobs-into-holes and ridges-into-grooves layers. Fig. 9. Coiled-coil spirals. For the phage coat proteins and flagellin, subunits are shown enlarged next to the structures, as well as the cross sections of the coiled-coil sheets they form. The positions of the subunits in the structures are indicated in white. The core packing layers are also shown for the phage coat proteins in order to illustrate the use of knobs-into-holes and ridges-into-grooves layers.
Another form of displayed peptide library is the FliTrx Random Peptide Display Library (Invitrogen, Paisley, UK), which uses the bacterial flagellum to display random peptide libraries on the E. coli cell surface (14). This library was constructed in the pFliTrx vector, which positions the random peptides in a flagellin (Fli) thioredoxin (Trx) fusion protein. Biopanning with bacteria works surprisingly well in our experience (15) and screening on nitrocellulose is similar to the Smith method. [Pg.135]

Lu, Z., Murray, K. S., Van Cleave, V., LaVallie, E. R., Stahl, M. L., and McCoy, J. M. (1995) Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin a system designed for exploring protein-protein interactions. Biotechnology 13, 366-372. [Pg.301]

Single O-linked residues of pseudaminic acid derivatives (or its enantiomer) modify flagellin, the major structural protein of the... [Pg.376]

Glycosylation of the proteins has the potential to influence the interaction of the cell with its environment. The presence of negatively charged pseudaminic acid derivatives on the surface would lower the isoelectric point, influence solubility, and likely increase ionic interactions.15 In C. jejuni flagellin, these may be further controlled by introduction of a basic acetamidino group to the sugar.16... [Pg.389]


See other pages where Flagellin protein is mentioned: [Pg.1100]    [Pg.394]    [Pg.395]    [Pg.521]    [Pg.158]    [Pg.1100]    [Pg.299]    [Pg.684]    [Pg.1100]    [Pg.394]    [Pg.395]    [Pg.521]    [Pg.158]    [Pg.1100]    [Pg.299]    [Pg.684]    [Pg.1207]    [Pg.395]    [Pg.266]    [Pg.27]    [Pg.248]    [Pg.455]    [Pg.1100]    [Pg.1101]    [Pg.1089]    [Pg.1090]    [Pg.1091]    [Pg.1091]    [Pg.1091]    [Pg.1091]    [Pg.1093]    [Pg.1831]    [Pg.3]    [Pg.10]    [Pg.382]    [Pg.382]    [Pg.389]    [Pg.389]    [Pg.397]    [Pg.398]    [Pg.399]   
See also in sourсe #XX -- [ Pg.394 ]

See also in sourсe #XX -- [ Pg.25 , Pg.394 ]




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Flagellin

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