Different populations of herpes simplex virus glycoprotein C discriminated by the carbohydrate-binding characteristics of N-acetylgalactosamine specific lectins (soybean and Helix pomatia). Brief report.
From the herpes simplex virus specified glycoprotein C two fractions were isolated with affinity either for Helix pomatia lectin (HPA) or soybean lectin (SBA). The data indicated that HPA and SBA, despite their mutual main specificity for N-acetylgalactosamine, recognize structurally different gC populations.
D000116:Acetylgalactosamine / Q000378:metabolism*; D005688:Galactosamine / Q000031:analogs & derivatives*; D037102:Lectins / Q000378:metabolism*; D037121:Plant Lectins; D018139:Simplexvirus / Q000032:analysis*; D030262:Soybean Proteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000032:analysis* / Q000378:metabolism; D010835:Phytohemagglutinins
D000116:Acetylgalactosamine; D005688:Galactosamine; D037102:Lectins; D037121:Plant Lectins; D030262:Soybean Proteins; D014759:Viral Envelope Proteins; D014764:Viral Proteins; C038095:Helix lectin; C038535:glycoprotein gC, herpes simplex virus type 1; C028824:soybean lectin; D010835:Phytohemagglutinins