Glycophorin as a receptor for Sendai virus

Leanne E. Wybenga, Raquel F. Epand, Shlomo Nir, Joseph W.K. Chu, Frances J. Sharom, Thomas D. Flanagan, Richard M. Epand*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

Glycophorin A was reconstituted into large unilamellar vesicles of egg phosphatidylcholine by detergent dialysis. The observed overall rate of Sendai virus fusion increased approximately 4-field between 0 and 0.006 mol % glycophorin, roughly proportional to the glycophorin content. However, no further increase in rate was observed at 0.02 mol % glycophorin. Treatment of reassembled glycophorin-liposomes with neuraminidase resulted in a significant decrease in the percent of vital fusion, confirming that the presence of sialic acid residues on glycophorin is essential for its role as a receptor. The sialic acid-containing glycolipid, the ganglioside GD(1a), was also incorporated into phosphatidylcholine liposomes, either in addition to or in place of glycophorin A. Comparing, on the basis of sialic acid content, liposomes containing either glycophorin or GD(1a), comparable rates and extents of fusion were found. However, on a molar basis glycophorin is much more effective. It was found that the addition of GD(1a), to glycophorin-containing liposomes only slightly increased the rate of fusion. This was largely due to an increase in the percent of virions capable of fusing.

Original languageEnglish
Pages (from-to)9513-9518
Number of pages6
JournalBiochemistry
Volume35
Issue number29
DOIs
StatePublished - 1996

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