Extensive Mammalian Ancestry of Pandemic (H1N1) 2009 Virus
Natalia A. Ilyushina1
, Jeong-Ki Kim1
, Nicholas J. Negovetich1
, Young-Ki Choi1
, Victoria Lang, Nicolai V. Bovin, Heather L. Forrest, Min-Suk Song, Philippe Noriel Q. Pascua, Chul-Joong Kim, Robert G. Webster
, and Richard J. Webby
Author affiliations: St. Jude Children’s Research Hospital, Memphis, Tennessee, USA (N.A. Ilyushina, J.-K. Kim, N.J. Negovetich, V. Lang, H.L. Forrest, R.G. Webster, R.J. Webby); D.I. Ivanovsky Institute of Virology, Moscow, Russia (N.A. Ilyushina); Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea (J.-K. Kim); Chungbuk National University College of Medicine and Medical Research Institute, Cheongju, Republic of Korea (Y.-K. Choi, M-S Song, P.N.Q. Pascua); Shemyakin Institute of Bioorganic Chemistry, Moscow (N.V. Bovin); Chungnam National University College of Veterinary Medicine, Daejeon (C.-J. Kim); University of Tennessee Health Science Center, Memphis (R.G. Webster, R.J. Webby)
Figure. Receptor specificity of human, pandemic, swine, and avian H1 influenza viruses. Association constants (Kass, 1/μM sialic acid) of virus complexes with sialylglycopolymers conjugated to 3′-sialyllactose (avian-like Neu5Acα2,3Gal-containing receptor, white bars) and 6′-sialyllactosamine (human-like Neu5Acα2,6Gal-containing receptor, black bars). Higher Kass values indicate stronger binding. Values are the mean ± SD of 4 independent experiments (1/μM sialic acid). 1, A/Brisbane/59/2007; 2, A/New Jersey/15/2007; 3, A/California/04/2009; 4, A/Tennessee/1-560/2009; 5, A/swine/North Carolina/007270/2008; 6, A/swine/Iowa/003479/2009; 7, A/mallard/Alberta/66/2007; 8, A/mallard/Alberta/496/2008.
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