Purification of virus glycoproteins by affinity chromatography using Lens culinaris phytohaemagglutinin

Abstract

The major components of the lipoprotein envelopes of many viruses are glycoproteins [l-5]. These glycoproteins are of considerable interest not only because of their structural and antigenic characteristics but also because their chemical properties may be typical of cell membrane glycoproteins in general. The release of these proteins from purified viruses is commonly achieved by either protease digestion or detergent solubilization [6-81. However, these procedures frequently cause denaturation or digestion of one or more of the envelope proteins and, furthermore, the separation of solubilized glycoproteins from the nonenvelope components of the viruses is often difficult to achieve. Recently, a method was described for the isolation of lymphocyte plasma membrane glycoproteins by means of affinity chromatography of sodium deoxycholate-solubilized membrane on LcH * covalently attached to Sepharose [9] ; LcH possesses antibody-like specificity for glucose, mannose and sterically related sugar residues [lo]. The present paper describes the application of this technique to the isolation of the envelope glycoproteins of a variety of viruses. The results demonstrate the value of this procedure in the identification and purification of virus glycoproteins and emphasize its general applicability to the separation of cell membrane glycoproteins.