1887

Abstract

SUMMARY

Purified Semliki Forest virus was analysed by analytical sedimentation, rate zonal sedimentation, isopycnic sedimentation, polyacrylamide gel electrophoresis and electron microscopy. It was found that the spherical virus particles had a sedimentation coefficient of 241 S (249 S determined by rate zonal sedimentation), and a buoyant density in sucrose of 1.190 g/ml; one protein and one glycoprotein were present in the virus; after fixation and negative staining with phosphotungstic acid the diameter of the particles was measured to be 50 to 56 nm. Treatment of Semliki Forest virus with 0.1% Tween 80 and 1% tri(-butyl)phosphate (TNBP) for 1 h at 4 °C destroyed infectivity and resulted in the appearance of the following haemagglutinating and immunizing virus components. (1) A spherical 211 S (217 S) component, 69 to 75 nm in diameter, consisting of an envelope and a core; one protein and one glycoprotein were present; the [H]-uridine:[C)-protein ratio was 2.8-fold higher than that of double-labelled untreated virus. (2) A spherical component, 70 to 73 nm in diameter, consisting of the virus envelope lacking intact cores; = 140 S (153 S); one glycoprotein was detected; the [H]-uridine: [C]-protein ratio was about 1/3 of untreated virus. (3) A 135 S component. (4) Structures assumed to represent envelope fragments; much of them had a sedimentation coefficient of 49 S. It was concluded from experiments with [H]-uridine-[C]-amino acids double-labelled and [C]-stearic acid-labelled virus that Tween 80-TNBP dissociates lipids and some protein components from the virus.

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1973-04-01
2022-01-16
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