The structural immunology of antibody protection against West Nile virus.
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.
Department of Molecular Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA. diamond@borcim.wustl.edu
Michael S
MS
Diamond
Theodore C
TC
Pierson
Daved H
DH
Fremont
D000818:Animals; D000914:Antibodies, Viral / Q000276:immunology*; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D006801:Humans; D017361:Viral Nonstructural Proteins / Q000276:immunology / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism; D014901:West Nile Fever / Q000276:immunology* / Q000517:prevention & control* / Q000821:virology; D014902:West Nile virus / Q000276:immunology*
D000914:Antibodies, Viral; D000939:Epitopes; C100315:NS1 protein, Flavivirus; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins