Adaptation of avian influenza A (H6N1) virus from avian to human receptor‐binding preference
Identifieur interne : 000622 ( Main/Exploration ); précédent : 000621; suivant : 000623Adaptation of avian influenza A (H6N1) virus from avian to human receptor‐binding preference
Auteurs : Fei Wang [République populaire de Chine] ; Jianxun Qi [République populaire de Chine] ; Yuhai Bi [République populaire de Chine] ; Wei Zhang [République populaire de Chine] ; Min Wang [République populaire de Chine] ; Baorong Zhang [République populaire de Chine] ; Ming Wang [République populaire de Chine] ; Jinhua Liu [République populaire de Chine] ; Jinghua Yan [République populaire de Chine] ; Yi Shi [République populaire de Chine] ; George F. Gao [République populaire de Chine]Source :
- The EMBO Journal [ 0261-4189 ] ; 2015-06-12.
Abstract
The receptor‐binding specificity of influenza A viruses is a major determinant for the host tropism of the virus, which enables interspecies transmission. In 2013, the first human case of infection with avian influenza A (H6N1) virus was reported in Taiwan. To gather evidence concerning the epidemic potential of H6 subtype viruses, we performed comprehensive analysis of receptor‐binding properties of Taiwan‐isolated H6 HAs from 1972 to 2013. We propose that the receptor‐binding properties of Taiwan‐isolated H6 HAs have undergone three major stages: initially avian receptor‐binding preference, secondarily obtaining human receptor‐binding capacity, and recently human receptor‐binding preference, which has been confirmed by receptor‐binding assessment of three representative virus isolates. Mutagenesis work revealed that E190V and G228S substitutions are important to acquire the human receptor‐binding capacity, and the P186L substitution could reduce the binding to avian receptor. Further structural analysis revealed how the P186L substitution in the receptor‐binding site of HA determines the receptor‐binding preference change. We conclude that the human‐infecting H6N1 evolved into a human receptor preference.
Historical analysis of influenza H6N1 isolates from 1972 until 2013, when the first human infection occurred, reveals amino acid changes that change receptor binding preference from birds to humans and therefore virus ability to cross the species barrier. Human‐infecting avian influenza H6N1 has gained human receptor binding preference. H6N1 HA has changed binding preference in at least two steps. First, E190V and G228S substitutions provide human receptor binding ability. Subsequently, P186L substitution reduces avian receptor binding, and provides human receptor binding preference.
Historical analysis of influenza H6N1 isolates from 1972 until 2013, when the first human infection occurred, reveals amino acid changes that change receptor binding preference from birds to humans and therefore virus ability to cross the species barrier.
Url:
- https://api.istex.fr/ark:/67375/WNG-HLXG82FZ-8/fulltext.pdf
- http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4475400
DOI: 10.15252/embj.201590960
Affiliations:
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<front><div type="abstract">The receptor‐binding specificity of influenza A viruses is a major determinant for the host tropism of the virus, which enables interspecies transmission. In 2013, the first human case of infection with avian influenza A (H6N1) virus was reported in Taiwan. To gather evidence concerning the epidemic potential of H6 subtype viruses, we performed comprehensive analysis of receptor‐binding properties of Taiwan‐isolated H6 HAs from 1972 to 2013. We propose that the receptor‐binding properties of Taiwan‐isolated H6 HAs have undergone three major stages: initially avian receptor‐binding preference, secondarily obtaining human receptor‐binding capacity, and recently human receptor‐binding preference, which has been confirmed by receptor‐binding assessment of three representative virus isolates. Mutagenesis work revealed that E190V and G228S substitutions are important to acquire the human receptor‐binding capacity, and the P186L substitution could reduce the binding to avian receptor. Further structural analysis revealed how the P186L substitution in the receptor‐binding site of HA determines the receptor‐binding preference change. We conclude that the human‐infecting H6N1 evolved into a human receptor preference.</div>
<div type="abstract">Historical analysis of influenza H6N1 isolates from 1972 until 2013, when the first human infection occurred, reveals amino acid changes that change receptor binding preference from birds to humans and therefore virus ability to cross the species barrier. Human‐infecting avian influenza H6N1 has gained human receptor binding preference. H6N1 HA has changed binding preference in at least two steps. First, E190V and G228S substitutions provide human receptor binding ability. Subsequently, P186L substitution reduces avian receptor binding, and provides human receptor binding preference.</div>
<div type="abstract">Historical analysis of influenza H6N1 isolates from 1972 until 2013, when the first human infection occurred, reveals amino acid changes that change receptor binding preference from birds to humans and therefore virus ability to cross the species barrier.</div>
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