Article

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

ABSTRACT

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.

Download full-text

Full-text

Available from: Amanda Balish
  • Source
    • "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. "
    [Show abstract] [Hide abstract]
    ABSTRACT: Wild ducks serve as the primary host for numerous and various influenza type A viruses. Occasionally, viruses from this reservoir can be transferred to other host species and cause outbreaks of influenza in fowl, swine, and horses, as well as result in novel human pandemics. Cellular tropism and range of susceptible host species are determined by interaction between virus and receptor molecules on cells. Here we discuss modern data regarding molecular features underlying interactions of influenza viruses with cellular receptors as well as a role for receptor specificity in interspecies transmission. By analyzing the earliest available pandemic influenza viruses (1918, 1957, 1968, 2009), we found that hemagglutinin reconfigured to recognize 2-6 sialic acid-containing receptors in the human upper airway tract together with altered enzymatic activity of neuraminidase necessary for maintaining functional balance with hemagglutinin are responsible for effective spread of influenza viruses in human populations. Resistance to low pH also contributes to this. Thus, a combination of such parameters makes it possible that influenza viruses give rise to novel pandemics.
    Full-text · Article · Jul 2015 · Biochemistry (Moscow)
  • Source
    • "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. "
    [Show abstract] [Hide abstract]
    ABSTRACT: This study brings the analysis of phylogenetic tree and amino acid sequences of Hemagglutinin (HA) from the influenza A virus that can infect a wide variety of birds and mammals. We have analyzed strains of three different years (2005, 2006 and 2007) of H5N1 from different country to see the antigenic shift patterns with respect to reported mutant positions of amino acids. We did not find the exact location where reported mutations are occurred. But we found similar amino acids near the reported mutated positions but we found similar mutations around the mutated position that may cause antigenic shifts.
    Full-text · Article · Jan 2015
  • Source
    • "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). "
    [Show abstract] [Hide abstract]
    ABSTRACT: It is reported that the H5N2 highly pathogenic avian influenza virus A/chicken/Hebei/1102/2010 (HB10) is a natural reassortant between circulating H5N1 and endemic H9N2 influenza viruses. To evaluate the potential of its interspecies transmission, the wild-type HB10 was adapted in mice through serial lung passages. Increased virulence was detectable in 5 sequential lung passages in mice and a highly virulent mouse-adapted strain (HB10-MA) with a 50% mouse lethal dose of 10(2.5) 50% egg infectious dose was obtained in 15 passages. The virulence and the replication efficiency of HB10-MA in mice were significantly higher than those of HB10 while HB10-MA grew faster and to significantly higher titers than HB10 in MDCK and A549 cells. Only five amino acid mutations in four viral proteins (HA-S227N, PB2-Q591K, PB2-D701N, PA-I554V and NP-R351K) of HB10-MA virus were found when compared with those of HB10, indicating that they may be responsible for the adaptation of the novel reassortant H5N2 avian influenza virus in mice with increased virulence and replication efficiency. The results in this study provide helpful insights into the pathogenic potential of novel reassortant H5N2 viruses to mammals that deserves further attentions.
    Full-text · Article · Jun 2014 · Veterinary Microbiology
Show more