Electrophoresis of measles virus on SDS-polyacrylamide gels demonstrated the presence of six polypeptides, two of which were glycoproteins. The glycoproteins were present on the surface of the virus and could be removed by treatment of the virus with bromelain. The released glycoprotein component contained H.A. antibody blocking activity but no haemolytic or cell fusion activities. Treatment of purified virus with Tween 20 solubilized the envelope glycoproteins and part of the envelope lipids. The solubilized envelope fragments had a sedimentation coefficient of 4 to 10S and contained H.A. antibody blocking activity and low H.A. activity. When the Tween 20 was removed by gel-filtration through Sephadex G200 the envelope fragments were shown to have haemolytic and cell-fusion activities. After equilibrium density centrifuging of the solubilized envelopes in CsCl the lipids remained at the top of the gradient and the glycoproteins which contained only H.A. activity banded at a buoyant density of 1.26 g/ml. However, haemolytic and cell-fusion activities could be regenerated after extensive dialysis of the glycoproteins with the virus lipid fraction or with phosphatidylethanolamine.


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