title: Valency of antibody binding to virions and its determination by surface plasmon resonance.
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.
authors.affiliation: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK. ndimmock@bio.warwick.ac.uk
authors.forename: Nigel J
authors.initials: NJ
authors.lastname: Dimmock
authors.forename: Sam A
authors.initials: SA
authors.lastname: Hardy
mesh_terms: D000914:Antibodies, Viral / Q000276:immunology / Q000378:metabolism*; D000915:Antibody Affinity; D001666:Binding Sites, Antibody; D007074:Immunoglobulin G / Q000276:immunology / Q000378:metabolism*; D009980:Influenza A virus / Q000276:immunology*; D020349:Surface Plasmon Resonance; D014771:Virion / Q000276:immunology*
chemical_list: D000914:Antibodies, Viral; D007074:Immunoglobulin G