2008
DOI: 10.1073/pnas.0801259105
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Contemporary North American influenza H7 viruses possess human receptor specificity: Implications for virus transmissibility

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Cited by 191 publications
(229 citation statements)
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“…Influenza viruses preferentially bind to glycans terminated by sialic acid, mostly Neu5Ac derivative, either Neu5Ac(α2→3)Gal or Neu5Ac(α2→6)Gal; human isolates predominantly bind to Neu5Ac(α2→6)Gal, while avian isolates mainly bind to Neu5Ac(α2→3)Gal [7,10,[33][34][35][36][37][38][39][40]. Glycan microarray analyses detected differences in human and avian influenza virus HA specificity, such as preferences for fucosylation and sialylation at positions 2 (Gal) and 3 (GlcNAc, GalNAc) of the terminal trisaccharide [41], and also showed that highly pathogenic avian influenza H5N1 viruses bind preferentially to Sia(α2→3)Gal structure [42] and highly pathogenic avian H7N7 viruses from The Netherlands in 2003 maintain the classic avian-binding preference for α2→3 linked sialic acids [43]. Recently, it was reported that a characteristic structural topology enables specific binding of HA to α2→6 sialylated glycans and human adapted H1N1 and H3N2 viruses specifically bind to long sialylated glycans containing tandem lactosamine structure such as Sia(α2→6)Gal(β1→4)GlcNAc (β1→3)Gal(β1→4)GlcNAc(β1→3)Gal-structures [10].…”
Section: Methodsmentioning
confidence: 99%
“…Influenza viruses preferentially bind to glycans terminated by sialic acid, mostly Neu5Ac derivative, either Neu5Ac(α2→3)Gal or Neu5Ac(α2→6)Gal; human isolates predominantly bind to Neu5Ac(α2→6)Gal, while avian isolates mainly bind to Neu5Ac(α2→3)Gal [7,10,[33][34][35][36][37][38][39][40]. Glycan microarray analyses detected differences in human and avian influenza virus HA specificity, such as preferences for fucosylation and sialylation at positions 2 (Gal) and 3 (GlcNAc, GalNAc) of the terminal trisaccharide [41], and also showed that highly pathogenic avian influenza H5N1 viruses bind preferentially to Sia(α2→3)Gal structure [42] and highly pathogenic avian H7N7 viruses from The Netherlands in 2003 maintain the classic avian-binding preference for α2→3 linked sialic acids [43]. Recently, it was reported that a characteristic structural topology enables specific binding of HA to α2→6 sialylated glycans and human adapted H1N1 and H3N2 viruses specifically bind to long sialylated glycans containing tandem lactosamine structure such as Sia(α2→6)Gal(β1→4)GlcNAc (β1→3)Gal(β1→4)GlcNAc(β1→3)Gal-structures [10].…”
Section: Methodsmentioning
confidence: 99%
“…The HPAI H7N7 virus NL/230 and the low-pathogenicity avian influenza (LPAI) H7N9 virus Shanghai/1, associated with human conjunctivitis and severe respiratory disease, respectively, are capable of transmission between ferrets in direct contact when inoculated i.n. (16,17). Following OA inoculation, both H7 viruses were transmitted to naïve ferrets in direct contact (Fig.…”
Section: Influenza Virus Transmissibility Following Oa Inoculationmentioning
confidence: 99%
“…75 On the other hand, some strains of LPAIV H9N2 and LPAIV and HPAIV of the H7 subtype that have crossed from avian to human hosts presented a2,6 receptor binding affinity, yet were apparently unable to transmit among humans. [76][77][78][79] Likewise, recombinant HPAIV H5N1 viruses displaying a2,6 receptor binding affinity replicated in the upper regions of the respiratory tract, yet were unable to transmit via aerosols in the ferret model. 80 Although a2,6 receptor binding affinity and replication to high viral titers in the upper regions of the respiratory tract may be necessary for efficient human-to-human transmission of influenza viruses, these characteristics are most likely not sufficient.…”
Section: Do Not Distributementioning
confidence: 99%