Selected article for: "antibody diversity and unique antibody"

Author: Rogers, J.; Schoepp, R.J.; Schröder, O.; Clements, T.L.; Holland, T.F.; Li, J.Q.; Li, J.; Lewis, L.M.; Dirmeier, R.P.; Frey, G.J.; Tan, X.; Wong, K.; Woodnutt, G.; Keller, M.; Reed, D.S.; Kimmel, B.E.; Tozer, E.C.
Title: Rapid discovery and optimization of therapeutic antibodies against emerging infectious diseases
  • Document date: 2008_5_13
  • ID: xkx56h0o_65
    Snippet: Using the HuFR TM approach, we isolated one humanized antibody (61H4) that had an equivalent ability compared to the chimera to neutralize SARS-CoV infection in Vero E6 cells and one (61G4) that demonstrated a 3.5-4-fold improvement in neutralization activity. Because the HuFR method combines heavy chains with different light chains, it generates a greater diversity of unique antibody combinations; potentially increasing the likelihood of finding.....
    Document: Using the HuFR TM approach, we isolated one humanized antibody (61H4) that had an equivalent ability compared to the chimera to neutralize SARS-CoV infection in Vero E6 cells and one (61G4) that demonstrated a 3.5-4-fold improvement in neutralization activity. Because the HuFR method combines heavy chains with different light chains, it generates a greater diversity of unique antibody combinations; potentially increasing the likelihood of finding beneficial humanized scaffolds. Thus, this method provides a comprehensive approach to humanizing antibodies without a loss in therapeutic function.

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