Hemagglutinin variants of influenza A(H1N1)pdm09 virus with reduced affinity for sialic acid receptors

Archives of Virology

Volumn 159, Issue 5, 2014, Pages 1207-1211

  Ayora Talavera, G ^a   Cetina Montejo, L ^a   Matos Patron A ^a   Romero Beltran L ^a  

^a UNIVERSIDAD AUTÓNOMA DE YUCATÁN   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; HEMAGGLUTININ; SIALIC ACID DERIVATIVE; SIALIC ACID RECEPTOR;

ARTICLE; GENE EXPRESSION REGULATION; GENETICS; INFLUENZA VIRUS A H1N1; METABOLISM; MUTATION; PHYSIOLOGY;

GENE EXPRESSION REGULATION, VIRAL; HEMAGGLUTININS; INFLUENZA A VIRUS, H1N1 SUBTYPE; MUTATION; RECEPTORS, CELL SURFACE; SIALIC ACIDS;

EID: 84899939365     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00705-013-1934-x     Document Type: Article

References (15)

1. Ayora-Talavera G, Shelton H, Scull MA, Ren J, Jones IM, Pickles RJ, Barclay WS (2009) Mutations in H5N1 influenza virus hemagglutinin that confer binding to human tracheal airway epithelium. PLoS One 4: e7836.
2. Chutinimitkul S, Herfst S, Steel J, Lowen AC, Jianqiang Y, van Riel D et al (2010) Virulence-associated substitution D222G in the hemagglutinin of 2009 pandemic influenza A(H1N1) virus affects receptor binding. J Virol 84: 11802-11813.
3. Gambaryan A, Robertson JS, Matrosovich MN (1999) Effects of egg-adaptation on the receptor-binding properties of human influenza A and B viruses. Virology 258: 232-239.
4. Gen F, Yamada S, Kato K, Akashi H, Kawaoka Y, Horimoto T (2013) Attenuation of an influenza A virus due to alteration of its hemagglutinin-neuraminidase functional balance in mice. Arch Virol 158: 1003-1011.
5. Glaser L, Stevens J, Zamarin D, Wilson IA, Garcia-Sastre A, Tumpey TM, Basler TC, Taubenberger JK, Palese P (2005) A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity. J Virol 79: 11533-11536.
6. Liu Y, Childs A, Matrosovich T, Wharton S, Palma AS, Chai W et al (2010) Altered receptor specificity and cell tropism of D222G hemagglutinin mutants isolated from fatal cases of pandemic A(H1N1)2009 influenza virus. J Virol 84: 12069-12074.
7. Matrosovich M, Tuzikov A, Bovin N, Gambaryan A, Klimov A, Castrucci MR, Donatelli I, Kawaoka Y (2000) Early alterations of the receptor-binding properties of H1, H2 and H3 avian influenza virus hemagglutinins after their introduction into mammals. J Virol 74: 8502-8512.
8. Ramos I, Krammer F, Hai R, Aguilera D, Bernal-Rubio D, Steel J, García-Sastre A, Fernandez-Sesma A (2013) H7N9 influenza viruses interact preferentially with α2, 3-linked sialic acids and bind weakly to α2, 6-linked sialic acids. J Gen Virol 94: 2417-2423.
9. Rykkvin R, Kilander A, Dudman SG, Hungnes O (2013) Within-patient emergence of the influenza A(H1N1)pdm09 HA1 222G variant and clear association with severe disease, Norway. Euro Surveill 18: 20369.
10. Stevens J, Blixt O, Glaser L, Taubenberger JK, Palese P, Paulson JC, Wilson IA (2006) Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J Mol Biol 355: 1143-1155.
11. Tumpey TM, Maines TR, van Hoeven N, Glaser L, Solorzano A, Pappas C, Cox NJ, Swayne DE, Palese P, Katz JM, Garcia-Sastre A (2007) A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission. Science 315: 655-659.
12. World Health Organization (2009) CDC protocol of realtime RTPCR for influenza A (H1N1).
13. World Health Organization (2009) Preliminary review of D222G amino acid substitution in the haemagglutinin of pandemic influenza A (H1N1) 2009 viruses.
14. Xu R, McBride R, Nycholat CM, Paulson JC, Wilson IA (2012) Structural characterization of the hemagglutinin receptor specificity from the 2009 H1N1 influenza pandemic. J Virol 86: 982-990.
15. Xu R, Zhu X, McBride R, Nycholat CM, Yu W, Paulson JC, Wilson IA (2012) Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic. J Virol 86: 9221-9232.