Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins.

@article{Shenoy2001SelectiveIO,
  title={Selective interactions of the human immunodeficiency virus-inactivating protein cyanovirin-N with high-mannose oligosaccharides on gp120 and other glycoproteins.},
  author={Shilpa R. Shenoy and Barry R O'Keefe and Anders Bolmstedt and Laura K Cartner and Michael R. Boyd},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={2001},
  volume={297 2},
  pages={704-10}
}
The virucidal protein cyanovirin-N (CV-N) mediates its highly potent anti-human immunodeficiency virus activity, at least in part, through interactions with the viral envelope glycoprotein gp120. Here we dissect in further detail the mechanism of CV-N's glycosylation-dependent binding to gp120. Isothermal titration calorimetry (ITC) binding studies of CV-N with endoglycosidase H-treated gp120 showed that binding was completely abrogated by removal of high-mannose oligosaccharides from the… CONTINUE READING