UNSPECIFIED (2004) Valency of antibody binding to virions and its determination by surface plasmon resonance. REVIEWS IN MEDICAL VIROLOGY, 14 (2). pp. 123-135. ISSN 1052-9276

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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 (C) 2004 John Wiley Sons, Ltd.

Item Type:	Journal Item
Subjects:	Q Science > QR Microbiology > QR355 Virology
Journal or Publication Title:	REVIEWS IN MEDICAL VIROLOGY
Publisher:	JOHN WILEY & SONS LTD
ISSN:	1052-9276
Official Date:	March 2004
Volume:	14
Number:	2
Number of Pages:	13
Page Range:	pp. 123-135
Identification Number:	10.1002/rmv.419
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/8640

Data sourced from Thomson Reuters' Web of Knowledge

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