OmniVira

Hemagglutinin receptor specificity and structural analyses of respiratory droplet-transmissible H5N1 viruses.

Robert P de Vries1 Xueyong Zhu Ryan McBride Alan Rigter Anthony Hanson Gongxun Zhong Masato Hatta Rui Xu Wenli Yu Yoshihiro Kawaoka Cornelis A M de Haan Ian A Wilson James C Paulson
Affiliations 1 institutions
  1. Departments of Cell and Molecular Biology and Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
PMID24173215 DOI10.1128/JVI.02690-13 Year2014 Journal Journal of virology J Virol Languageeng Statusppublish

Abstract

Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" α2-6 sialosides but with notable differences in fine specificity. Crystal structure analysis further shows that the stalk mutation causes no obvious perturbation of the receptor-binding pocket, consistent with its impact on hemagglutinin stability without affecting receptor specificity.

Supporting text Virus Host Location
Hemagglutinins 24 Humans 1440 Influenza A Virus, H5N1 Subtype 300

Evidence records

2 total
Functional Mechanism
2 records · 2 evidence types
Evidence type Receptor Usage
1 records
OVE1625 Receptor Usage
Key finding

Ferret-adapted H5N1 viruses capable of respiratory droplet transmission show a shift toward binding human-type α2-6 sialoside receptors.

Virus
Influenza A virus H5N1
Host
domestic ferret Mustela putorius furo Experimental system
Location
Not specified
Supporting text

Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to "human-type" α2-6 sialosides but with notable differences in fine specificity.

Method
glycan microarray analysis
Receptors
α2-6 sialosides
Evidence type Molecular Adaptation
1 records
OVE1626 Molecular Adaptation
Key finding

Mutations in the hemagglutinin receptor-binding site and stalk domains of H5N1 are associated with adaptation for respiratory droplet transmission in ferrets through altered receptor binding to human-type α2-6 sialosides.

Virus
Influenza A virus H5N1
Host
Not specified
Location
Not specified
Supporting text

Two ferret-adapted H5N1 viruses capable of respiratory droplet transmission have been reported with mutations in the hemagglutinin receptor-binding site and stalk domains. Glycan microarray analysis reveals that both viruses exhibit a strong shift toward binding to human-type α2-6 sialosides.

Genes or proteins
hemagglutinin
Receptors
α2-6 sialosides
Mutations
mutations in the receptor-binding site | stalk domain mutation
Mechanism types
receptor binding | transmission fitness | host-range expansion