title: H10N8 and H6N1 maintain avian receptor binding.
abstract: Influenza viruses of animals can cross species and infect humans. In this issue of Cell Host & Microbe, Zhang et al. (2015) and Tzarum et al. (2015) describe crystal structures and receptor-binding properties of hemagglutinins of avian-origin H10N8 and H6N1 influenza viruses. Human infections with these viruses are not associated with a switch favoring human receptor binding.
authors.affiliation: Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam 3015 GE, the Netherlands.
authors.forename: Mathilde
authors.initials: M
authors.lastname: Richard
authors.affiliation: Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam 3015 GE, the Netherlands. Electronic address: r.fouchier@erasmusmc.nl.
authors.forename: Ron A M
authors.initials: RAM
authors.lastname: Fouchier
mesh_terms: D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D065926:Influenza A Virus, H10N8 Subtype / Q000502:physiology*; D009980:Influenza A virus / Q000737:chemistry* / Q000502:physiology*; D007251:Influenza, Human / Q000821:virology*; D011991:Receptors, Virus / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*; D053585:Virus Attachment
chemical_list: D019267:Hemagglutinin Glycoproteins, Influenza Virus; D011991:Receptors, Virus; D012794:Sialic Acids