H10N8 and H6N1 maintain avian receptor binding

Mathilde Richard; Ron A M Fouchier

doi:10.1016/j.chom.2015.02.020

H10N8 and H6N1 maintain avian receptor binding

Cell Host Microbe. 2015 Mar 11;17(3):292-294. doi: 10.1016/j.chom.2015.02.020.

Authors

Mathilde Richard¹, Ron A M Fouchier²

Affiliations

¹ Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam 3015 GE, the Netherlands.
² Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam 3015 GE, the Netherlands. Electronic address: r.fouchier@erasmusmc.nl.

PMID: 25766290
DOI: 10.1016/j.chom.2015.02.020

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.

Publication types

Comment

MeSH terms

Hemagglutinin Glycoproteins, Influenza Virus / chemistry*
Hemagglutinin Glycoproteins, Influenza Virus / metabolism*
Humans
Influenza A Virus, H10N8 Subtype / physiology*
Influenza A virus / chemistry*
Influenza A virus / physiology*
Influenza, Human / virology*
Receptors, Virus / metabolism*
Sialic Acids / metabolism*
Virus Attachment*

Substances

Hemagglutinin Glycoproteins, Influenza Virus
Receptors, Virus
Sialic Acids