Search results for: Mouse Anti-Rubella Virus Glycoprotein E2
#17905485 
2007/09/14
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Semliki Forest virus vectors expressing the H and HN genes of measles and mumps viruses reduce immunity induced by the envelope protein genes of rubella virus.
A Semliki Forest virus (SFV) recombinant particle vaccine vector was constructed expressing the viral E1 and E2 envelope proteins of the RA27/3 vaccine strain of rubella virus. This vector induced high titres of antibody after intramuscular administration to Balb/C mice, both following initial vaccination and a boost 4 weeks later. This occurred for antibody as measured by ELISA and as measured by a latex agglutination test. However, co-administration of similar particles expressing the measles virus H protein and the mumps virus HN protein with the rubella protein expressing vector resulted in reduction of the anti-rubella immune response.Sara J Callagy, Barbara J Kelly, Marina N Fleeton, Brian J Sheahan, Sareen E Galbraith, Gregory J Atkins
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Purification of rubella virus E1-E2 protein complexes by immunoaffinity chromatography.
A murine monoclonal antibody directed against the E1 membrane glycoprotein of rubella virus was immobilized on an N-hydroxysuccinimide-activated chromatographic support. The antibody was used to purify rubella virus E1-E2 protein complexes from Tween-80/diethyl ether extracts of cell culture supernatants containing virus particles. The adsorption behaviour of immunosorbents with ligand densities of 2.9, 5.4 and 11.1 mg monoclonal antibody per millilitre of gel was investigated using batchwise conditions. Then the immunoaffinity purification process was optimized with regard to adsorption efficiency by adjusting the flow rate, the bed height and the amount of sample loaded onto the column. The optimized immunoaffinity purification process which is reproducible and relatively simple (one-step) had a yield of 73%, a concentration factor of 5-8 and a purification factor of about 2600. No mouse IgG due to ligand leakage could be detected in the immunopurified product using an enzyme immunoassay. High-performance size exclusion chromatography, sodium dodecyl sulphate polyacrylamide gel electrophoresis, immunoblotting and electron microscopy showed that the immunopurified product contained rosette-like structures formed by complexes of E1 and E2 proteins. The product retained its hemagglutinating activity and proved to be suitable for application in a fluorescent enzyme immunoassay for determination of anti-rubella IgG in human serum.A P van Sommeren, P A Machielsen, W J Schielen, H P Bloemers, T C Gribnau