Sign up & Download
Sign in

A haemagglutinin (HA1)-specific FAb neutralizes influenza A virus by inhibiting fusion activity

by M. J. Edwards, N. J. Dimmock
Journal of General Virology ()

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 virus 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.

Cite this document (BETA)

Available from www.ncbi.nlm.nih.gov
Page 1
hidden
Page 2
hidden

Readership Statistics

20 Readers on Mendeley
by Discipline
 
 
 
by Academic Status
 
40% Other Professional
 
30% Researcher (at a non-Academic Institution)
 
15% Post Doc

Sign up today - FREE

Mendeley saves you time finding and organizing research. Learn more

  • All your research in one place
  • Add and import papers easily
  • Access it anywhere, anytime

Start using Mendeley in seconds!

Already have an account? Sign in