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F Nadon

Publications and source records attributed to F Nadon.

23 records · Page 2Linked to original sources
PubMed1985

E1 glycoprotein of rubella virus carries an epitope that binds a neutralizing antibody.

We identified by immunoprecipitation and Western blot analysis, using a monoclonal antibody that neutralizes rubella virus, that E1 glycoprotein carries an epitope linked with neutralization. Glycosidase treatment of virus does not prevent blotting of this monoclonal antibody with the E1 glycoprotein, dissociating this epitope from the hemagglutination epitope which is linked with the oligosaccharide side chains. We also investigated by Western blot analysis human serum reactivity toward E1 glycoprotein and the two other structural proteins of rubella virus, E2 and C: all positive sera detected E1 and C, irrespective of their titers, indicating the importance of glycoprotein E1 in immunity. Frequent lack of reactivity against E2 might suggest that this glycoprotein is either less exposed or less immunogenic.

Antibodies, Monoclonal↗
PubMed1982

Antibody response to rubella virus proteins in different physical forms.

The immunogenicity of different antigens, containing rubella virus hemagglutinating (HA) membrane protein, was studied using live virus, beta-propiolactone-inactivated virus, detergent and lipid-free octamers and virosomes. Whole virus particles, live or inactivated, induced hemagglutination inhibition (HAI) antibodies in rabbits after one subcutaneous injection of 0.16 micrograms of HA protein. Hemagglutinin rosettes or virosomes failed to induce antibodies even at a dose of 120 micrograms. Apparently, the extraction of viral membrane hemagglutinin, for the preparation of a rubella subunit vaccine, led to destruction of the antigenicity responsible for the induction of hemagglutination inhibiting antibodies. These results are discussed in the light of earlier studies on the preparation of a rubella subunit vaccine.

Animals↗
PubMed1981

Virosome preparation: differences between influenza and rubella hemagglutinin adsorption.

Rubella and influenza virosomes were prepared from preformed liposomes or dried lipid films with or without nonionic detergent beta-D-octylglucoside. The preformed liposomes and lipid films were prepared from lecithin and dicetyl phosphate (3.5:1). Viral hemagglutinin rosettes were prepared from purified viruses after solubilization with Triton X-100 (1%), centrifugation through a continuous sucrose gradient containing 30 mM octylglucoside, and dialysis. Analysis of virosomes by sucrose density gradient centrifugation, hemagglutination assay, and electron microscopy revealed that rubella hemagglutinin did not require the presence of detergent to form virosomes, whereas influenza hemagglutinin could absorb efficiently to liposomes only in the presence of detergent.

Adsorption↗