The molecular basis of antibody-mediated neutralization of West Nile virus.
The study of the interaction between the West Nile virus envelope protein and monoclonal antibodies has provided insight into the molecular mechanisms of neutralization. Structural studies have identified an epitope on the lateral ridge of domain III of the West Nile virus E protein that is recognized by antibodies with the strongest neutralizing activity in vitro and in vivo. Antibodies that bind to this epitope are particularly inhibitory because they block infection at a post-attachment step and at concentrations that result in a low occupancy of the available sites on the virion.
Oliphant
Theodore
T
Washington University School of Medicine, Department of Molecular Microbiology, Saint Louis, MO 63110, USA.
Diamond
Michael S
MS
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology* / Q000627:therapeutic use; D000914:Antibodies, Viral / Q000276:immunology*; D000915:Antibody Affinity; D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D000956:Antigens, Viral / Q000737:chemistry / Q000276:immunology*; D018604:Epitope Mapping; D006801:Humans; D008958:Models, Molecular; D009500:Neutralization Tests; D011487:Protein Conformation; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000276:immunology*; D014901:West Nile Fever / Q000188:drug therapy / Q000276:immunology; D053060:West Nile Virus Vaccines / Q000276:immunology* / Q000627:therapeutic use; D014902:West Nile virus / Q000276:immunology*
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000956:Antigens, Viral; D014759:Viral Envelope Proteins; D053060:West Nile Virus Vaccines