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Volume 23, Number 2—February 2017
Research

Highly Pathogenic Influenza A(H5Nx) Viruses with Altered H5 Receptor-Binding Specificity

Hongbo Guo1, Erik de Vries1, Ryan McBride, Jojanneke Dekkers, Wenjie Peng, Kim M. Bouwman, Corwin Nycholat, M. Helene Verheije, James C. Paulson, Frank J.M. van Kuppeveld, and Cornelis A.M. de HaanComments to Author 
Author affiliations: Utrecht University, Utrecht, the Netherlands (H. Guo, E. de Vries, J. Dekkers, K.M. Bouwman, M.H. Verheije, F.J.M. van Kuppeveld, C.A.M. de Haan); The Scripps Research Institute, La Jolla, California, USA (R. McBride, W. Peng, C. Nycholat, J.C. Paulson)

Main Article

Figure 1

Binding of influenza A virus hemagglutinins to A) fetuin and B) transferrin. Limiting dilutions of soluble H5 trimers complexed with horseradish peroxidase−conjugated antibodies were used in a fetuin- or transferrin-binding assay. Optical density at 450 nm (OD450) corresponds to binding of HA to glycoproteins. HA, hemagglutinin; H5N12.3.4, novel H5N1 virus clade 2.3.4; H5N11, H5N1 virus clade 1.

Figure 1. Binding of influenza A virus hemagglutinins to A) fetuin and B) transferrin. Limiting dilutions of soluble H5 trimers complexed with horseradish peroxidase−conjugated antibodies were used in a fetuin- or transferrin-binding assay. Optical density at 450 nm (OD450) corresponds to binding of HA to glycoproteins. HA, hemagglutinin; H5N12.3.4, novel H5N1 virus clade 2.3.4; H5N11, H5N1 virus clade 1.

Main Article

1These authors contributed equally to this article.

Page created: January 17, 2017
Page updated: January 17, 2017
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