PMID: 6168285Aug 6, 1981Paper

Studies on the interaction of Sendai virus with liposomal membranes. Sendai virus-induced agglutination of liposomes containing glycophorin

Biochimica Et Biophysica Acta
N OkuK Inoue

Abstract

Liposomes constituted with the major sialoglycoprotein of human erythrocytes, glycophorin, were used as models for studies on cell-virus interactions. Liposomes composed of egg yolk phosphatidylcholine, cholesterol and glycophorin were found to interact with the paramyxovirus HVJ to form aggregates. The aggregation process was temperature dependent: it was maximal at 0 degrees C and decreased with increase of the incubation temperature. The activity of viral neuraminidase is also temperature dependent, and it increases with increase of the incubation temperature; release of N-acetylneuraminic acid was negligible at 0 degrees C. Shift-up of the incubation temperature immediately cancelled HVJ-induced agglutination of liposomes. Viruses attached to liposomes seemed to be released into the supernatant when the 'virus-liposome' complex formed at 0 degrees C was incubated at 37 degrees C, possibly as a result of breakdown of the 'binding' site by neuraminidase. The characteristics of the interaction of HVJ with liposomes containing glycophorin appeared to be phenomenologically similar to those of HVJ-cell interaction.

References

Oct 1, 1975·The Journal of General Virology·A M Haywood
Mar 15, 1974·Journal of Molecular Biology·A M Haywood
Dec 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·C W Grant, H M McConnell
Aug 15, 1974·Journal of Molecular Biology·A M Haywood
Aug 1, 1971·Hoppe-Seyler's Zeitschrift für physiologische Chemie·W StoffelT S Tschung

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Citations

Apr 1, 2006·Glycoconjugate Journal·Enrique Villar, Isabel Muñoz Barroso
Mar 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·C E KundrotR I MacDonald
Jan 1, 1987·Membrane Biochemistry·D P Sarkar, R Blumenthal

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