In contrast to other viral glycoproteins, the herpes simplex virus (HSV) glycoprotein C (gC) binds to the -acetylgalactosamine-specific lectin (HPA). In the present paper gC was purified by affinity chromatography with monospecific antibodies and the purified glycoprotein was subjected to protease digestion. HPA-binding protease-resistant glycopeptides were isolated by lectin affinity chromatography. The isolated structures did not bind to concanavalin A and seemed to lack charged groups as determined by ion-exchange chromatography. In gel filtration, the glycopeptides appeared in two peaks with molecular weights higher than 4000. The HPA-binding structures of gC were synthesized in the presence of tunicamycin, indicating that they belong to the -glycosyl class of oligosaccharides. In addition to HPA-binding oligosaccharides, synthesis of tunicamycin-resistant wheat germ lectinbinding gC oligosaccharides was demonstrable. These were sensitive to sialidase and apparently unrelated to the HPA-binding oligosaccharides.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error