West Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.

@article{Chung2006WestNV,
  title={West Nile virus nonstructural protein NS1 inhibits complement activation by binding the regulatory protein factor H.},
  author={Kyung Min Chung and M. Kathryn Liszewski and Grant E. Nybakken and Alan E. Davis and R. Reid Townsend and Daved H. Fremont and John P Atkinson and Michael S Diamond},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2006},
  volume={103 50},
  pages={19111-6}
}
The complement system, by virtue of its dual effector and priming functions, is a major host defense against pathogens. Flavivirus nonstructural protein (NS)-1 has been speculated to have immune evasion activity, because it is a secreted glycoprotein, binds back to cell surfaces, and accumulates to high levels in the serum of infected patients. Herein, we demonstrate an immunomodulatory function of West Nile virus NS1. Soluble and cell-surface-associated NS1 binds to and recruits the complement… CONTINUE READING
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