The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.

@article{Olofsson1999TheRO,
  title={The role of a single N-linked glycosylation site for a functional epitope of herpes simplex virus type 1 envelope glycoprotein gC.},
  author={S. Olofsson and Anders Bolmstedt and Marlene Biller and Kristina M{\aa}rdberg and Johan Leckner and Bo G. Malmstr{\"o}m and Edward Trybala and Tomas Bergstr{\"o}m},
  journal={Glycobiology},
  year={1999},
  volume={9 1},
  pages={73-81}
}
A monoclonal antibody, B1C1, binding to an epitope of antigenic site II of the herpes simplex virus type 1 (HSV-1) glycoprotein gC-1, is a potent inhibitor of two important biological functions of gC-1: its binding to cell surface heparan sulfate and its binding to the receptor for complement factor C3b. Here, we have analyzed a B1C1-resistant HSV-1 variant… CONTINUE READING