Recent investigations of the interaction between the West Nile virus (WNV) envelope protein (E) and monoclonal antibodies (mAbs) have elucidated fundamental insights into the molecular mechanisms of neutralization. Structural studies have defined an epitope on the lateral ridge of domain III (DIII-lr) of the WNV E protein that is recognized by antibodies with the strongest neutralizing activity in vitro and in vivo. Antibodies that bind this epitope are highly potent because they efficiently block at a post-entry step of viral infection with relatively low virion occupancy requirements. In this review, we discuss the structural, molecular, and immunologic basis for antibody-mediated protection against WNV, and its implications for novel therapeutic or vaccine strategies.

Original languageEnglish
Pages (from-to)212-225
Number of pages14
JournalImmunological Reviews
Issue number1
StatePublished - Oct 2008


  • Antibodies
  • Antigens/peptides/epitopes
  • Complement
  • Emerging infectious disease
  • Infectious diseases


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