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Cholera toxin B subunit

Luppi P. H Aston-Jones G Akaoka H., Chouvet G., Jouvet M. (1995). Afferent projections to the rat locus coeruleus demonstrated by retrograde and anterograde tracing with cholera-toxin B subunit and Phaseolus vulgaris leucoagglutinin. Neuroscience 65(1), 119-60. [Pg.216]

Kenworthy, A. K., Petranova, N. and Edidin, M. (2000). High resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol. Biol. Cell 11, 1645-55. [Pg.70]

J. P. Thompson and C.-L. Schengrund, Oligosaccharide-derivatized dendrimers Defined multivalent inhibitors of the adherence of the cholera toxin B subunit and the heat labile enterotoxin of E. coli to GM1, Glycoconjug. J., 14 (1997) 837-845. [Pg.389]

CP coat protein CtxB cholera toxin B subunit scFv single chain Fv antibody fragment TMOF trypsin modulating oostatic factor MAB monoclonal antibody GFP green fluorescent protein CPV Canine parvovirus BHV Bovine herpes virus FMDV Foot and mouth disease virus HCV Hepatitis C virus HRV Human rhino Virus MEV Mink enteritis virus MHV Murine hepatitis virus MV Measles virus RSV Respiratory syncytial virus... [Pg.79]

Cholera toxin B subunit CaMV 35S promoter/ nos terminator Kozak sequence, KDEL Lycopersicon esculentum Leaves 0.02% ofTSP Fruits 0.04% ofTSP 45... [Pg.96]

To highlight the caveolae pathway, a couple of substances are discussed and applied. The most commonly used markers besides the SV40 (17,20) are probably cholera toxin B subunit (CtxB) and caveolin-1-GFP. Folate and... [Pg.356]

Jani D, Meena LS, Mohammad Q, Haq R, Singh Y, Sharma AK, Tyagi AK. (2002) Expression of cholera toxin B subunit in transgenic tomato plants. [Pg.652]

Li D, O Leary J, Huang Y, Huner NPA, Jevnikar AM, Ma S. (2006) Expression of cholera toxin B subunit and the B chain of human insulin as a fusion protein in transgenic tobacco plants. Plant Cell Rep 25 417-424. [Pg.652]

NT008 Jani, D., N. K. Singh, S. Bhattacharya, et al. Studies on the immunogenic potential of plant-expressed cholera toxin B subunit. Plant Cell Rep 2004 22(7) 471-477. [Pg.340]

Since plastids have a limited set of protein degradation pathways, foreign proteins that exhibit harmful effects to the plant in the cytoplasm may be more stable when they accumulate within the chloroplast (Heifetz, 2000). For example, the vaccine protein cholera toxin B subunit was shown to be toxic even when it accumulated to very low levels within the plant cytoplasm, but was nontoxic when it accumulated to large quantities within the chloroplast. Plastids also possess the ability to form disulfide bonds, a requirement for many correctly folded mammalian proteins (Daniell et al., 2005a). These properties have made them attractive for the production of biopharmaceuticals in plants. [Pg.65]

Daniell, H., Lee, S.-B., Panchal, T., and Wiebe, P.O. (2001). Expression of the native cholera toxin B subunit gene and assembly as functional oligomers in transgenic tobacco chloroplasts. J. Mol. Biol. 311 1001-1009. [Pg.75]

Liposomes MTP-PE liposomes IL-7 liposomes cholera toxin-B subunit expressed liposomes IL-2 liposome [69-73]... [Pg.322]

Cholera toxin B subunit GM-1 Mouse epithelial cells and tissues [95,96]... [Pg.366]

Fig. 18.2. Biosensor scheme describing the various steps involved in the immunoassay using ITO-poly(pyrrole-biotin)-coated optical fibers for the detection of anti-cholera toxin B subunit using the biotin-avidin immobilization technique. Fig. 18.2. Biosensor scheme describing the various steps involved in the immunoassay using ITO-poly(pyrrole-biotin)-coated optical fibers for the detection of anti-cholera toxin B subunit using the biotin-avidin immobilization technique.
Fig. 18.7. Schematic representation of the immobilization of the biotinylated cholera toxin B subunit using the biotin-avidin bridging system. The hydrophilic co-polymer on the transducer surface improves the permeation of the enzymatically generated quinone. Fig. 18.7. Schematic representation of the immobilization of the biotinylated cholera toxin B subunit using the biotin-avidin bridging system. The hydrophilic co-polymer on the transducer surface improves the permeation of the enzymatically generated quinone.
Cholera toxin B subunit-biotin labeled (lyophilized powder, biotin content 0.9mol/mol protein), peroxidase-labeled IgG anti-rabbit antibody (HRP-Ab, from goat, protein content 0.8mg/ml, affinity isolated antibody), anti-cholera toxin (from rabbit, protein content 48mg/ml, purified toxin from Vibrio cholerae), biotin monoclonal anti-rabbit IgG -y-chain specific (from mouse, protein content 4.2mg/ml), glucose oxidase-biotinamidocaproyl labeled (GOX-B, from Aspergillus niger, lyophilized powder containing 40-70% protein, 137 U/mg), polyoxyeth-ylene-sorbitan monolaurate (Tween 20), bovine serum albumin (fraction... [Pg.1134]

Intravaginal vaccination with whole cell and cholera toxin B subunit (CTB) oral cholera vaccine provided a greater success rate in providing a mucosal immune response in the female genital tract than an oral vaccination [152]. This study demonstrated that in a single individual, systemic immunity did not directly reflect the local antibody response in the mucosal... [Pg.424]

Johansson, E.L., et al. 1998. Antibodies and antibody secreting cells in the female genital tract after vaginal or intranasal immunization with cholera toxin B subunits or conjugate. Infect Immunol 66 514. [Pg.469]

Cholera toxin B subunit + Vaccin) (first 3 years)... [Pg.199]

Robinson HL (2007) HIV/AIDS vaccines 2007. Clin Pharmacol Ther 82(6) 686-693 Roland KL, Cloninger C, Kochi SK, Thomas LJ, Tinge SA, Rouskey C, Killeen KP (2007) Construction and preclinical evaluation of recombinant Peru-15 expressing high levels of the cholera toxin B subunit as a vaccine against enterotoxigenic Escherichia coli. Vaccine 25(51) 8574-8584... [Pg.220]

After 1 hour of treatment, fluorescent transferrin can be localized in early endosomes and the endosomal-recycling compartment, whereas the cholera toxin B-subunit distinctly traffics to the trans-golgi network of living cells. In cells treated with holo-cholera toxin comprising the B-subunit and the catalytic A-subunit, the toxin would traffic further to the endoplasmic reticulum, which would enable the release of the toxic A-subunit into the cytoplasm. [Pg.386]


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See also in sourсe #XX -- [ Pg.115 ]

See also in sourсe #XX -- [ Pg.324 ]




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