UNSPECIFIED (1994) COMPETITIVE-BINDING OF NEUTRALIZING MONOCLONAL AND POLYCLONAL IGG TO THE HA OF INFLUENZA-A VIRIONS IN SOLUTION - ONLY ONE IGG MOLECULE IS BOUND PER HA TRIMER REGARDLESS OF THE SPECIFICITY OF THE COMPETITOR. VIROLOGY, 205 (1). pp. 360-363. ISSN 0042-6822

Full text not available from this repository.

Abstract

Two-step solution competition assays were performed in solution with influenza type A virions and hemagglutinin (HA)specific neutralizing monoclonal antibodies (mabs), These demonstrated that the binding of one molecule of IgG mab per HA trimer prevented the binding of mabs directed against other antigenic sites on the HA (site A, site B, or site D), even though these are topographically separate and antigenically independent. Furthermore the same procedures showed that one molecule of mab per trimer prevented the binding of polyclonal HA-specific IgG obtained from the serum of rabbits immunized with whole virus. This restricted binding is clearly a property of the intact virion, since others using purified HA have shown that up to four IgG molecules of different specificities can bind per trimer. Since the surface area of the globular head of the trimer is equivalent to approximately 10 nonoverlapping antibody footprints, it is not understood how one prebound IgG molecule prevents the binding of other IgG molecules. (C) 1994 Academic Press, Inc.

Item Type:	Journal Item
Subjects:	Q Science > QR Microbiology > QR355 Virology
Journal or Publication Title:	VIROLOGY
Publisher:	ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS
ISSN:	0042-6822
Date:	15 November 1994
Volume:	205
Number:	1
Number of Pages:	4
Page Range:	pp. 360-363
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/20205

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item