Treatment of Sendai virus with 0.3% tri(-butyl)phosphate and 0.1% Tween 80 led to the disintegration of virus envelopes and to the formation of envelope-derived particles (EP) consisting of ‘rosettes’ endowed with surface projections and of spikeless envelope remnants. EP had a higher buoyant density in CsCl gradients than intact virus (1.29 compared with 1.20 g/cm); their sedimentation coefficient was 190 S. EP agglutinated red blood cells and contained neuraminidase. Their haemolytic activity was greatly increased in comparison with intact virus. Three virus polypeptides and traces of an additional protein were detected in EP by polyacrylamide gel electrophoresis. EP retained approximately 30% of choline-containing phospholipids present in the virus envelope. The haemolytic activity of EP and of intact virus was destroyed by treatment with either trypsin or diisopropylfluorophosphate. Insolubilised trypsin failed to alter the haemolytic activity. Proteolytic cleavage of RBC membrane components occurred during haemolysis.


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