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Haemagglutinin of Measles Virus: Purification and Storage with Preservation of Biological and Immunological Properties

¹ INSERM U218, Centre Léon Bérard, 69373 Lyon Cedex 08
and² Laboratoire de Biologie Moléculaire et Cellulaire, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon Cedex 07, France

Measles virus envelope haemagglutinin (H) was purified rapidly with Triton X-100-solubilized virions by a two-step anion-exchange chromatography using fast protein liquid chromatography. The purity of the glycoprotein in its dimeric form was demonstrated by SDS-PAGE followed by silver staining or autoradiography. The purified H glycoprotein was further freed from contaminating detergent by dialysis of octylglucoside detergent. This purification procedure, together with subsequent lyophilization and storage at -70°C of the H glycoprotein which was incorporated into phospholipid vesicles allowed the full preservation of its haemagglutinating activity, its reactivity with a monoclonal anti-H antibody that recognized a conformational epitope and its capacity to elicit anti-H antibodies with haemagglutination-inhibiting and neutralizing activities.

Keywords: measles virus, haemagglutinin, purification

Received 17 March 1988; accepted 9 May 1988.

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