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

AUTOR(ES)

Olofsson, S

RESUMO

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.

Documentos Relacionados

• Primate cytomegalovirus glycoproteins: lectin-binding properties and sensitivities to glycosidases.
• Surface properties of extracellular malaria parasites: electrophoretic and lectin-binding characteristics.
• Characterization of Caenorhabditis Elegans Lectin-Binding Mutants
• Identification of lectin-binding proteins in Chlamydia species.
• Herpes simplex virus type 1-specific immunity induced by peptides corresponding to an antigenic site of glycoprotein B.