Unusual lectin-binding properties of a herpes simplex virus type 1-specific glycoprotein

Abstract

Lysates from herpes simplex virus type 1(HSV-1)-infected [green monkey kidney AH-1 and hamster kidney BHK-21] cells were subjected to affinity chromatography on soybean and Helix pomatia lectins. One of the virus-specified glycoproteins, probably the HSV-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 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.