We report a simple method for the isolation of the measles virus glycoproteins, and their subsequent incorporation into artificial lipid bilayers. The two viral glycoprotins, HA and F, were isolated in preparative amounts from disrupted purified virus by lentil lectin affinity chromatography. The proteins were reconstituted into single bilayer lipid vesicles by: (i) exchanging the non-dialysable detergent Nonidet P40 (NP40) for a dialysable one, octylglucoside, while the proteins were immobilized on the lectin column and (ii) co-dialysis of the eluted glycoproteins in octylglucoside with phosphatidylcholine. The resultant ‘virosomes’ had visible ‘spikes’ and possessed haemagglutinating activity. These measles virosomes should provide a useful reagent for studying immune responses to measles virus, independent of the immunosuppressive effects of the whole virus.


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