tetano
Editor, Senior Moderator
Vet Microbiol
. 2020 Jun;245:108669.
doi: 10.1016/j.vetmic.2020.108669. Epub 2020 Apr 30.
A D200N Hemagglutinin Substitution Contributes to Antigenic Changes and Increased Replication of Avian H9N2 Influenza Virus
Jingwei Song[SUP] 1 [/SUP], Chenxi Wang[SUP] 1 [/SUP], Weihua Gao[SUP] 1 [/SUP], Haoran Sun[SUP] 1 [/SUP], Zhimin Jiang[SUP] 1 [/SUP], Kaijing Wang[SUP] 1 [/SUP], Xiaolei Ren[SUP] 1 [/SUP], Zejiang Wang[SUP] 1 [/SUP], Qi Tong[SUP] 1 [/SUP], Mingyang Wang[SUP] 1 [/SUP], Honglei Sun[SUP] 1 [/SUP], Yipeng Sun[SUP] 1 [/SUP], Jinhua Liu[SUP] 1 [/SUP], Juan Pu[SUP] 2 [/SUP]
Affiliations
Abstract
Influenza virus hemagglutinin (HA) plays an important role in viral antigenicity, replication and host range. However, few amino acid positions in HA were reported to play multiple functions in both viral antigenicity and replication. In the present study, through analyzing the amino acid sequences of H9N2 avian influenza viruses (AIVs) isolated from China, we identified a multi-functional substitution of D200N in HA1 protein. Firstly, the substitution of D200N changed the antigenicity of H9N2 AIVs. Secondly, the D200N increased the HA cleavage efficiency and reduced acid and thermal stability of HA protein, which triggered viral-endosomal membrane fusion whereby promoted the release of viral genome into the host cytoplasm. Finally, residue 200-N increased the replication of H9N2 viruses in both chicken embryo fibroblast (CEF) cells and chicken embryonated eggs. In summary, the D200N substitution is a newly identified antigenicity and replication determinant of H9N2 AIVs, which should be paid more attention during surveillance.
Keywords: Acid and thermal stability; Antigenicity; H9N2 avian influenza virus; HA substitution; Replication.
. 2020 Jun;245:108669.
doi: 10.1016/j.vetmic.2020.108669. Epub 2020 Apr 30.
A D200N Hemagglutinin Substitution Contributes to Antigenic Changes and Increased Replication of Avian H9N2 Influenza Virus
Jingwei Song[SUP] 1 [/SUP], Chenxi Wang[SUP] 1 [/SUP], Weihua Gao[SUP] 1 [/SUP], Haoran Sun[SUP] 1 [/SUP], Zhimin Jiang[SUP] 1 [/SUP], Kaijing Wang[SUP] 1 [/SUP], Xiaolei Ren[SUP] 1 [/SUP], Zejiang Wang[SUP] 1 [/SUP], Qi Tong[SUP] 1 [/SUP], Mingyang Wang[SUP] 1 [/SUP], Honglei Sun[SUP] 1 [/SUP], Yipeng Sun[SUP] 1 [/SUP], Jinhua Liu[SUP] 1 [/SUP], Juan Pu[SUP] 2 [/SUP]
Affiliations
- PMID: 32456831
- DOI: 10.1016/j.vetmic.2020.108669
Abstract
Influenza virus hemagglutinin (HA) plays an important role in viral antigenicity, replication and host range. However, few amino acid positions in HA were reported to play multiple functions in both viral antigenicity and replication. In the present study, through analyzing the amino acid sequences of H9N2 avian influenza viruses (AIVs) isolated from China, we identified a multi-functional substitution of D200N in HA1 protein. Firstly, the substitution of D200N changed the antigenicity of H9N2 AIVs. Secondly, the D200N increased the HA cleavage efficiency and reduced acid and thermal stability of HA protein, which triggered viral-endosomal membrane fusion whereby promoted the release of viral genome into the host cytoplasm. Finally, residue 200-N increased the replication of H9N2 viruses in both chicken embryo fibroblast (CEF) cells and chicken embryonated eggs. In summary, the D200N substitution is a newly identified antigenicity and replication determinant of H9N2 AIVs, which should be paid more attention during surveillance.
Keywords: Acid and thermal stability; Antigenicity; H9N2 avian influenza virus; HA substitution; Replication.