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Valency of antibody binding to virions and its determination by surface plasmon resonance

✍ Scribed by Nigel J. Dimmock; Sam A. Hardy

Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
242 KB
Volume
14
Category
Article
ISSN
1052-9276

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✦ Synopsis

Abstract

All IgGs are homobivalent, but their ability to bind bivalently to the surface of a virus particle depends mainly on a favourable spacing of cognate epitopes and the angle that the FAb arm makes with the virus surface. If the angle of binding forces the second FAb arm to point into solution, monovalent binding is inevitable. This IgG will have the same affinity as its FAb, will be less stably bound than if it were bound bivalently, cannot cross‐link epitopes on the surface of a virion, and cannot neutralise by cross‐linking surface proteins. However, at moderate IgG concentrations, monovalently bound IgG can reduce infectivity by aggregating virions, a phenomenon that cannot occur with IgG bound bivalently. This review describes how surface plasmon resonance can be used to determine the valency of IgG binding to enveloped and non‐enveloped virus particles, and discusses the implications of this new methodology. Copyright © 2004 John Wiley & Sons, Ltd.

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