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

Resultado de la investigación: Articlerevisión exhaustiva

4 Citas (Scopus)

Resumen

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.

Idioma originalEnglish (US)
Páginas (desde-hasta)161-171
Número de páginas11
PublicaciónJournal of General Virology
Volumen54
N.º1
DOI
EstadoPublished - ene 1 1981
Publicado de forma externa

ASJC Scopus subject areas

  • Virology

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