A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity.

@article{Fromme2007AMM,
  title={A monovalent mutant of cyanovirin-N provides insight into the role of multiple interactions with gp120 for antiviral activity.},
  author={Raimund Fromme and Zivile Katiliene and Barbara Giomarelli and Federica Bogani and James Mc Mahon and Toshiyuki Mori and Petra Fromme and Giovanna Ghirlanda},
  journal={Biochemistry},
  year={2007},
  volume={46 32},
  pages={9199-207}
}
Cyanovirin-N (CV-N) is a 101 amino acid cyanobacterial lectin with potent antiviral activity against HIV, mediated by high-affinity binding to branched N-linked oligomannosides on the viral surface envelope protein gp120. The protein contains two carbohydrate-binding domains, A and B, each of which binds short oligomannosides independently in vitro. The interaction to gp120 could involve either a single domain or both domains simultaneously; it is not clear which mode would elicit the antiviral… CONTINUE READING