The molecular basis of antibody-mediated neutralization of West Nile virus

Theodore Oliphant; Michael S. Diamond

doi:10.1517/14712598.7.6.885

The molecular basis of antibody-mediated neutralization of West Nile virus

Theodore Oliphant, Michael S. Diamond

Research output: Contribution to journal › Review article › peer-review

16 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	885-892
Number of pages	8
Journal	Expert opinion on biological therapy
Volume	7
Issue number	6
DOIs	https://doi.org/10.1517/14712598.7.6.885
State	Published - Jun 2007

Keywords

Affinity
Antibody
Antibody-dependent enhancement
Epitope
Neutralization
West Nile virus

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10.1517/14712598.7.6.885

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title = "The molecular basis of antibody-mediated neutralization of West Nile virus",

abstract = "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.",

keywords = "Affinity, Antibody, Antibody-dependent enhancement, Epitope, Neutralization, West Nile virus",

author = "Theodore Oliphant and Diamond, {Michael S.}",

note = "Funding Information: The authors would like to thank K Austin and G Nybakken for help with figure preparation and D Fremont and T Pierson for helpful discussions. Work in our laboratory is supported by the Pediatric Dengue Vaccine Initiative and the NIH (grants AI061373 and U54 AI057160).",

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AU - Diamond, Michael S.

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N2 - 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.

AB - 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.

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KW - Antibody

KW - Antibody-dependent enhancement

KW - Epitope

KW - Neutralization

KW - West Nile virus

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JO - Expert opinion on biological therapy

JF - Expert opinion on biological therapy

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ER -

The molecular basis of antibody-mediated neutralization of West Nile virus

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Keywords

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