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Volume 24, Number 7—July 2018
Research

Diversity of Influenza A(H5N1) Viruses in Infected Humans, Northern Vietnam, 2004–2010

Hirotaka Imai1, Jorge M. Dinis1, Gongxun Zhong, Louise H. Moncla, Tiago J.S. Lopes, Ryan McBride, Andrew J. Thompson, Wenjie Peng, Mai thi Q. Le, Anthony Hanson, Michael Lauck, Yuko Sakai-Tagawa, Shinya Yamada, Julie Eggenberger, David H. O’Connor, Yasuo Suzuki, Masato Hatta, James C. Paulson, Gabriele Neumann, and Yoshihiro KawaokaComments to Author 
Author affiliations: University of Wisconsin, Madison, Wisconsin, USA (H. Imai, J.M. Dinis, G. Zhong, L.H. Moncla, T.J.S. Lopes, A. Hanson, M. Lauck, J. Eggenberger, D.H. O’Connor, M. Hatta, G. Neumann, T.C. Friedrich, Y. Kawaoka); The Scripps Research Institute, La Jolla, California, USA (R. McBride, A.J. Thompson, W. Peng, J.C. Paulson); National Institute of Hygiene and Epidemiology, Hanoi, Vietnam (M.t.Q. Le); University of Tokyo, Tokyo, Japan (Y. Sakai-Tagawa, S. Yamada, Y. Kawaoka); Chubu University, Kasugai, Japan (Y. Suzuki)

Main Article

Figure 4

Effect of amino acid variations in HA on virus thermostability in influenza A(H5N1) virus isolates from humans, northern Vietnam, 2004–2010. A) Amino acid substitutions in non–receptor-binding domains mapped on the 3-dimensional structure of the monomer of VN1203 HA (Protein Data Bank accession no. 2FK0). Red indicates modeled human-type receptor; purple indicates positions of amino acid variations on the non–receptor-binding domains; blue indicates positions of amino acid variations on the rece

Figure 4. Effect of amino acid variations in HA on virus thermostability in influenza A(H5N1) virus isolates from humans, northern Vietnam, 2004–2010. A) Amino acid substitutions in non–receptor-binding domains mapped on the 3-dimensional structure of the monomer of VN1203 HA (Protein Data Bank accession no. 2FK0). Red indicates modeled human-type receptor; purple indicates positions of amino acid variations on the non–receptor-binding domains; blue indicates positions of amino acid variations on the receptor-binding domain corresponding to Figure 2, panel A. B–G) Thermostability of HA variants depicted in panel A. Amounts of viruses equivalent to 64 HA units were incubated at 55°C for 15, 30, 60, 120, and 240 min. B–D) HA titers in heat-treated samples were determined by performing HA assays with 0.5% turkey red blood cells: B) CA04/UT31312II-HA, CA04/UT31312II-HA-92K, CA04/UT31312III-HA, CA04/VN1203; C) CA04/UT31394II-HA, CA04/UT31394II-HA-54(+1)E, CA04/UT31394II-HA-67T, CA04/VN1203; D) CA04/K173. E–G) Virus titers of heat-treated samples determined by means of plaque assays in MDCK cells. Shown are the mean HA or virus titers of triplicates from a single experiment. Dashed lines indicate the detection limit for virus titration (20 PFU/mL). E) CA04/UT31312II-HA, CA04/UT31312II-HA-92K, CA04/UT31312III-HA, CA04/VN1203; F) CA04/UT31394II-HA, CA04/UT31394II-HA-54(+1)E, CA04/UT31394II-HA-67T, CA04/VN1203; G) CA04/K173. CA04/K173 virus was used as a control. HA, hemagglutinin.

Main Article

1These authors contributed equally to this article.

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