Hemagglutinin Receptor Binding of a Human Isolate of Influenza A(H10N8) Virus - Volume 21, Number 7—July 2015 - Emerging Infectious Disease journal - CDC
Volume 21, Number 7—July 2015
Hemagglutinin Receptor Binding of a Human Isolate of Influenza A(H10N8) Virus
Human infections with avian influenza A(H10N8) virus were reported in China during the 2013–14 winter influenza season. The first patient, a 73-year old woman, became ill in November 2013 a few days after visiting a live poultry market in Jiangxi Province (1). Two additional patients, a 55-year-old woman and a 75-year-old man, were admitted to hospitals in the same province in January 2014 (2). Severe pneumonia and subsequent acute respiratory distress syndrome developed in all 3 patients; 2 of the patients died, 5 and 6 days after admission (2).
Epithelial cells of the human upper respiratory tract contain mostly α2,6-linked sialic acids (SAα2,6) and low levels of α2,3-linked sialic acids (SAα2,3) (3). Hemagglutinin (HA) of avian influenza virus strains shows preferential binding to SAα2,3 receptors, which partially accounts for the reduced ability of avian influenza strains to establish infections in humans (3). Interaction with SAα2,6 receptors is one of the requirements for efficient replication in the human upper respiratory tract. In addition, reduced binding to SAα2,3 facilitates respiratory droplet-based transmission in ferrets (4). Therefore, emerging avian influenza viruses with increased binding to SAα2,6 and reduced binding to SAα2,3 pose a major pandemic threat, and active research and surveillance to detect animal viruses with modified receptor binding are warranted.
Dr. Ramos is an assistant professor in the Department of Microbiology at the Icahn School of Medicine at Mount Sinai, New York, NY. Her main research interests focus on receptors for influenza viruses and innate immunity to these viruses.
We thank CFG for providing reagents. Some of the data will be published on the CFG website (http://www.functionalglycomics.org/). We also thank the Flow Cytometry Shared Facility and the Microscopy Core Facility at Icahn School of Medicine at Mount Sinai for assistance, the Icahn School of Medicine Institutional Biorepository for providing human tissue sections, John Steel and Randy A. Albrecht for providing recombinant influenza viruses, and GISAID for making H10N7 and H10N8 subtype virus sequencing data publicly available.
This study was supported by the National Institutes of Health/National Institute of Allergy and Infectious Diseases (Center for Research on Influenza Pathogenesis, contract HHSN272201400008C to J.A.R., F.K., and A.F.-S.) as part of the Centers for Excellence for Influenza Research and Surveillance Network. I.R. was partially supported by National Institutes of Health training grant T32 AI788926.
- Chen H, Yuan H, Gao R, Zhang J, Wang D, Xiong Y, Clinical and epidemiological characteristics of a fatal case of avian influenza A H10N8 virus infection: a descriptive study. Lancet. 2014;383:714–21 .
- Zhang W, Wan J, Qian K, Liu X, Xiao Z, Sun J, Clinical characteristics of human infection with a novel avian-origin influenza A(H10N8) virus. Chin Med J (Engl). 2014;127:3238–42 .
- Neumann G, Kawaoka Y. Host range restriction and pathogenicity in the context of influenza pandemic. Emerg Infect Dis. 2006;12:881–6 .
- Tumpey TM, Maines TR, Van Hoeven N, Glaser L, Solorzano A, Pappas C, A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission. Science. 2007;315:655–9 .
- Zohari S, Neimanis A, Harkonen T, Moraeus C, Valarcher JF. Avian influenza A(H10N7) virus involvement in mass mortality of harbour seals (Phoca vitulina) in Sweden, March through October 2014. Euro Surveill. 2014;19:20967 .
- Watanabe T, Kiso M, Fukuyama S, Nakajima N, Imai M, Yamada S, Characterization of H7N9 influenza A viruses isolated from humans. Nature.2013;501:551–5 .
- Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem. 2000;69:531–69 .
- Vachieri SG, Xiong X, Collins PJ, Walker PA, Martin SR, Haire LF, Receptor binding by H10 influenza viruses. Nature. 2014;511:475–7 .
- Ramos I, Bernal-Rubio D, Durham N, Belicha-Villanueva A, Lowen AC, Steel J, Effects of receptor binding specificity of avian influenza virus on the human innate immune response. J Virol. 2011;85:4421–31 .
- Ramos I, Krammer F, Hai R, Aguilera D, Bernal-Rubio D, Steel J, H7N9 influenza viruses interact preferentially with alpha2,3-linked sialic acids and bind weakly to alpha2,6-linked sialic acids. J Gen Virol. 2013;94:2417–23 .
- Krammer F, Margine I, Tan GS, Pica N, Krause JC, Palese P. A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates. PLoS ONE. 2012;7:e43603 .
- Tharakaraman K, Jayaraman A, Raman R, Viswanathan K, Stebbins NW, Johnson D, Glycan receptor binding of the influenza A virus H7N9 hemagglutinin. Cell. 2013;153:1486–93 .
- Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J. Structure and receptor binding preferences of recombinant hemagglutinins from avian and human H6 and H10 influenza A virus subtypes. J Virol. 2015 Feb 11;pii: JVI.03456-14.
- Wang M, Zhang W, Qi J, Wang F, Zhou J, Bi Y, Structural basis for preferential avian receptor binding by the human-infecting H10N8 avian influenza virus. Nat Commun. 2015;6:5600.
- Beare AS, Webster RG. Replication of avian influenza viruses in humans. Arch Virol. 1991;119:37–42 .
Suggested citation for this article: Ramos I, Mansour M, Wohlbold TJ, Ermler ME, Hirsh A, Runstadler JA, et al. Hemagglutinin receptor binding of a human isolate of influenza A(H10N8) virus. Emerg Infect Dis. 2015 Jul [date cited]. http://dx.doi.org/10.3201/eid2107.141755