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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 6

Binding of influenza A virus mutant H5N12.3.4 HA (A) and H5N8 HA (B) to fetuin. Binding was assayed as described in the legend to Figure 1. Mutated residues are indicated. 160/222/227, 160/193/222/227, and 160/193/199/222/227 refer to T160A/K222Q/S227R, T160A/K193N/K222Q/S227R and T160A/K193N/T199D/K222Q/S227R substitutions in H5N12.3.4 HA, respectively. Optical density at 450 nm (OD450) corresponds to binding of HA to glycoproteins. WT, wild-type; HA, hemagglutinin. H5N12.3.4, novel H5N1 virus

Figure 6. Binding of influenza A virus mutant H5N12.3.4 HA (A) and H5N8 HA (B) to fetuin. Binding was assayed as described in the legend to Figure 1. Mutated residues are indicated. 160/222/227, 160/193/222/227, and 160/193/199/222/227 refer to T160A/K222Q/S227R, T160A/K193N/K222Q/S227R and T160A/K193N/T199D/K222Q/S227R substitutions in H5N12.3.4 HA, respectively. Optical density at 450 nm (OD450) corresponds to binding of HA to glycoproteins. WT, wild-type; HA, hemagglutinin. H5N12.3.4, novel H5N1 virus clade 2.3.4.

Main Article

1These authors contributed equally to this article.

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