Purification of measles virus glycoproteins and their integration into artificial lipid membranes

P. Casali, J. G. Patrick Sissons, R. S. Fujinami, M. B.A. Oldstone

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

We report a simple method for the isolation of the measles virus glycoproteins, and their subsequent incorporation into artifical lipid bilayers. The two viral glycoproteins, HA and F, were isolated in preparative amounts from disrupted purified virus lentil lectin affinity chromatography. The proteins were reconstituted into single bilayer lipid vesicles by: (i) exchanging the non-dialysable detergent Nonidet P40 (NP40) for a dialysable one, octylglucoside, while the proteins were immobilized on the lectin column and (ii) co-dialysis of the eluted glycoproteins in octylglucoside with phosphatidylcholine. The resultant 'virosomes' had visible 'spikes' and possessed haemagglutinating activity. These measles virosomes should provide a useful reagent for studying immune responses to measles virus, independent of the immunosuppressive effects of the whole virus.

Original languageEnglish (US)
Pages (from-to)161-171
Number of pages11
JournalJournal of General Virology
Volume54
Issue number1
DOIs
StatePublished - Jan 1 1981
Externally publishedYes

ASJC Scopus subject areas

  • Virology

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