Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein.
Lysates from herpes simplex virus type 1-infected cells were subjected to affinity chromatography on soybean and Helix pomatia lectins. One of the virus-specified glycoproteins, probably the herpes simplex virus type 1-specific gC glycoprotein, bound to the lectins and was eluted with N-acetylgalactosamine. The affinity chromatography permitted a high degree of purification of the type-specific glycoprotein with respect to both host cell components and other viral glycoproteins. The lectin affinity pattern of this glycoprotein indicates the presence of a terminal alpha-N-acetylgalactosamine in an oligosaccharide, a finding not reported previously for glycoproteins of enveloped viruses.
D000956:Antigens, Viral / Q000032:analysis; D002846:Chromatography, Affinity; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D006372:Helix, Snails; D037102:Lectins; D037121:Plant Lectins; D018139:Simplexvirus / Q000032:analysis*; D013025:Glycine max; D014764:Viral Proteins / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*
D000956:Antigens, Viral; D006023:Glycoproteins; D037102:Lectins; D037121:Plant Lectins; D014764:Viral Proteins