UNSPECIFIED (2001) A haemagglutinin (HA1)-specific FAb neutralizes influenza A virus by inhibiting fusion activity. JOURNAL OF GENERAL VIROLOGY, 82 (Part 6). pp. 1387-1395. ISSN 0022-1317

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Abstract

H9-D3-4R2 (referred to as H9), a murine monoclonal HA1-specific IgG3, recognizes an epitope within antigenic site Cb of influenza virus A/PR/8/34 (H1N1). At 50% neutralization, inhibition of virus-mediated fusion was responsible for the majority of neutralization but, at higher antibody concentrations, the attachment of vi rus to target cells was also inhibited and may have contributed to neutralization. H9 FAb was also neutralizing, although the concentration needed was two orders of magnitude greater than for the IgG, Functional affinity of the IgG and affinity of the FAb were almost identical, and it is not clear why the neutralization efficiency of the FAb was so low. Unlike its IgG, H9 FAb had no detectable effect on virus attachment but inhibited virus fusion activity. It thus appears that monovalent binding by this antibody is sufficient to inhibit fusion activity and that this was directly responsible for neutralization of infectivity.

Item Type:	Journal Article
Subjects:	T Technology > TP Chemical technology Q Science > QR Microbiology > QR355 Virology
Journal or Publication Title:	JOURNAL OF GENERAL VIROLOGY
Publisher:	SOC GENERAL MICROBIOLOGY
ISSN:	0022-1317
Date:	June 2001
Volume:	82
Number:	Part 6
Number of Pages:	9
Page Range:	pp. 1387-1395
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/12138

Data sourced from Thomson Reuters' Web of Knowledge

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