%0 Journal Article %A Olofsson, Sigvard %A Lundström, Marita %A Marsden, Howard %A Jeansson, Stig %A Vahlne, Anders %T Characterization of a Herpes Simplex Virus Type 2-specified Glycoprotein with Affinity for N-Acetylgalactosamine-specific Lectins and Its Identification as g92K or gG %D 1986 %J Journal of General Virology, %V 67 %N 4 %P 737-744 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-67-4-737 %K HSV-2 %K Helix pomatia lectin %K N-acetylgalactosamine %K glycoprotein G %I Microbiology Society, %X Summary 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 × 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-67-4-737