Journal
IMMUNOLOGICAL REVIEWS
Volume 225, Issue -, Pages 212-225Publisher
WILEY
DOI: 10.1111/j.1600-065X.2008.00676.x
Keywords
infectious diseases; antibodies; emerging infectious disease; antigens/peptides/epitopes; complement
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Funding
- Pediatric Dengue Vaccine Initiative
- Burroughs Wellcome Fund
- NIAID of the NIH [U01 AI061373, U54 AI057160, R01 AI073755]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [ZIAAI001022, U01AI061373, U54AI057160, R01AI073755] Funding Source: NIH RePORTER
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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.
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