Gambaryan, A. S. et al. Evolution of the receptor binding phenotype of influenza A (H5) viruses. Virology 344, 432-438

Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, 142782 Moscow, Russia.
Virology (Impact Factor: 3.32). 02/2006; 344(2):432-8. DOI: 10.1016/j.virol.2005.08.035
Source: PubMed


Receptor specificity of influenza A/H5 viruses including human 2003-04 isolates was studied. All but two isolates preserved high affinity to Sia2-3Gal (avian-like) receptors. However, two isolates (February, 2003, Hong Kong) demonstrated decreased affinity to Sia2-3Gal and moderate affinity to a Sia2-6Gal (human-like) receptors. These two viruses had a unique Ser227-Asn change in the hemagglutinin molecule. Thus, a single amino acid substitution can significantly alter receptor specificity of avian H5N1 viruses, providing them with an ability to bind to receptors optimal for human influenza viruses. Asian 2003-04 H5 isolates from chickens and humans demonstrated highest affinity to the sulfated trisaccharide Neu5Acalpha2-3Galbeta1-4(6-HSO3)GlcNAcbeta (Su-3'SLN) receptor but, in contrast to 1997 isolates, had increased affinity to fucosylated Su-3'SLN. American poultry H5 viruses also had increased affinity to Su-3'SLN. These data demonstrate that the genetic evolution of avian influenza A(H5N1) viruses is accompanied during adaptation to poultry by the evolution of their receptor specificity.

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    • "However, several cases of the disease were noted in communities when such transmission probably took place. In particular, several family members become sick in 2003, and the influenza virus isolated from them possessed a Ser227Asn mutation in the receptor-binding site and had sharply decreased affinity to Siaα2-3Gal-terminated receptors and acquired ability to bind 6′SLN[40,41]. Stevens et al. investigated changes in receptor phenotype of H5N1 influenza viruses resulting from " classic " mutations responsible for recognition of Siaα2-6Gal by human influenza viruses[42]. It was demonstrated that the Glu190Asp substitution worsened its binding to Siaα2-3Gal, and Gly225Asp substitution did not affect it, whereas combined action of these mutations completely disrupted binding to any receptors. "
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    • "We found some avian amino acid position Q222L[35], G224S (35), S227N[33], Q192H[34]are specific to SAα 2, 3 Gal receptor which has a previous reported history to affect human. On the other hand there are some avian amino acid position S227N[33,37], Q192H[34], N186K[37], Q196R[36], N182K[38], Q192R[38], S223N[39], G228S[36,40]are specific to SAα2, 6 Gal receptor which has a previous reported history to affect human. In our avian H5N1 analysis we did not find the exact location where reported mutations are occurred. "
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    • "In this study, comparison of the predicted amino acid sequences of HB10-MA and HB10 viruses demonstrated five substitutions involving four of the ten viral proteins. Mouseadapted HB10-MA virus acquired a S227N mutation within the binding site, and this position is considered to have a reduced binding affinity toward SA2, 3 Gal and an increased affinity toward SA2, 6 Gal (Gambaryan et al., 2006), it together with the removal of the 158N glycosylation (Yen et al., 2009), resulted in more-efficient viral replication in the upper respiratory tract of ferrets and serum antibody response. The PB2 gene is important for the virulence of HPAI H5N1 and H7N7 viruses and the transmission of H1N1/1918 virus (Hatta et al., 2001). "
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