1. Intact F glycoprotein is required to induce permeability changes in Lettrée cells or in erythrocytes. Some HN glycoproteins may also be required. Permeability changes thus offer a simple, accurate and rapid means of assaying the integrity of F glycoprotein in certain viral preparations. 2. The ‘1-day’ virus (which contains intact F glycoprotein but which differs morphologically from ‘3 day’ virus) does not cause permeability changes; it can be rendered active by various physical treatments. It is concluded that the environment in which F glycoprotein is embedded is a determining factor for permeability changes. 3. The entry of fluorescently labelled peptides into cells made permeable by virus has been measured. Peptides having a molecular weight in excess of 1000 enter poorly, suggesting a ‘pore’ size of approx. 1 nm in diameter. 4. Two novel assay methods concerned with virus—cell fusion are described. The first measures the fluorescence enhancement that occurs when anthroylstearate is transferred from anthroylstearate-labelled virus to cells. The second measures the giant-cell formation that occurs when partially fused erythrocytes are exposed to hypo-osmotic treatment. The ‘1-day’ virus is active in these assays. In contrast with permeability changes, virus—cell fusion is insensitive to changes in external Ca2+-concentration. 5. The results are compatible with a model [Knutton & Pasternak (1979) Trends Biochem. Sci. 4, 220—223; Impraim, Foster, Micklem & Pasternak (1980) Biochem. J. 186, 847—860] in which virus—cell fusion is a prerequisite for permeability changes, and in which permeability changes are the cause of haemolysis and giant-cell (polykaryon) formation.
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Research Article| September 15 1980
Components involved in virally mediated membrane fusion and permeability changes
Biochem J (1980) 190 (3): 625–638.
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A M Wyke, C C Impraim, S Knutton, C A Pasternak; Components involved in virally mediated membrane fusion and permeability changes. Biochem J 15 September 1980; 190 (3): 625–638. doi: https://doi.org/10.1042/bj1900625
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