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Department of Virology, Institute of Medical Microbiology, University of Göteborg, Guldhedsgatan 10 B, S-413 46 Göteborg, Sweden
and1 Institute of Virology, University of Glasgow, Church Street, Glasgow G11 5JR, U.K.
Extracts from herpes simplex virus type 2 (HSV-2)-infected cells were subjected to affinity chromatography with gel-bound Helix pomatia lectin (HPA). Only one HSV-2-specified glycoprotein was isolated by this procedure and the glycoprotein had an apparent molecular weight of 130000 (130K). The HPA-binding glycoprotein was genetically mapped, using HSV-1 x HSV-2 intertypic recombinants into the short component of the HSV-2 genome. The mapping position, electrophoretic mobility and the antigenic properties of the HPA-binding protein indicated that it was unrelated to glycoprotein C (gC), which is the HPA-binding glycoprotein in HSV-1-infected cells, and distinct from gE and gD which map in the S component. The glycoprotein was almost quantitatively precipitated by monoclonal antibody AP1, specific for glycoprotein g92K and it also reacted with monoclonal antibody 1206-3, specific for the HSV-2 glycoprotein G previously described. It is concluded that the isolated glycoprotein is identical to g92K and consequently also to the HSV-2-specific glycoprotein G.
Keywords: HSV-2, glycoprotein G, N-acetylgalactosamine, Helix pomatia lectin
Received 7 October 1985;
accepted 31 December 1985.
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