Mutations of 127, 183 and 212 residues on the HA globular head affect the antigenicity, replication and pathogenicity of H9N2 avian influenza virus

被引:9
作者
Fan, Menglu [1 ,2 ]
Liang, Bing [1 ,2 ]
Zhao, Yongzhen [1 ,2 ]
Zhang, Yaping [3 ]
Liu, Qingzheng [1 ,2 ]
Tian, Miao [1 ,2 ]
Zheng, Yiqing [1 ,2 ]
Xia, Huizhi [1 ,2 ]
Suzuki, Yasuo [4 ]
Chen, Hualan [3 ]
Ping, Jihui [1 ,2 ]
机构
[1] Nanjing Agr Univ, MOE Int Joint Collaborat Res Lab Anim Hlth & Food, Nanjing 210095, Peoples R China
[2] Nanjing Agr Univ, Jiangsu Engn Lab Anim Immunol, Coll Vet Med, Nanjing 210095, Peoples R China
[3] CAAS, Harbin Vet Res Inst, State Key Lab Vet Biotechnol, Harbin, Peoples R China
[4] Chubu Univ, Coll Life & Hlth Sci, Kasugai, Aichi, Japan
基金
中国国家自然科学基金;
关键词
antigenicity; avian influenza A virus; glycosylation; pathogenicity; HEMAGGLUTININ GLYCOSYLATION; POULTRY; NEURAMINIDASE; TRANSMISSION; EVOLUTION; VIRULENCE; BINDING; ALTERS; MUTANT; H5;
D O I
10.1111/tbed.14363
中图分类号
R51 [传染病];
学科分类号
100401 ;
摘要
H9N2 avian influenza virus (AIV), one of the predominant subtypes devastating the poultry industry, has been circulating widely in the poultry population and causing huge economic losses. In this study, two H9N2 viruses with similar genetic backgrounds but different antigenicity were isolated from a poultry farm, namely A/chicken/Jiangsu/75/2018 (JS/75) and A/chicken/Jiangsu/76/2018 (JS/76). Sequence analysis revealed that their surface genes differed in three amino acid residues (127, 183 and 212) on the head of hemagglutinin (HA). To explore the differences between the two viruses in their biological features, six recombinant viruses, including the wild-type or mutant HA and NA of JS/75 and JS/76 were generated with A/Puerto Rico/8/1934 (PR8) backbone via reverse genetics. The chicken challenge study and HI assay data indicated that r-76/PR8 showed the most obvious antigen escape due to 127 and 183 amino acid substitutions in HA gene. Further studies verified that the 127N site was glycosylated in JS/76 and its mutants. Receptor-binding assays showed that all the recombination viruses were prone to bind the human-like receptors, except for the mutants which glycosylated 127N was deleted. Growth kinetics and mice challenge experiments indicated that 127N-glycosylated viruses showed less replication in A549 cells and lower pathogenicity in mice compared with wild-type viruses. Therefore, the glycosylation site and two amino acid alternations in the HA globular head were responsible for the differences in antigenicity and pathogenicity between the two H9N2 isolates. This study is significant in the research of the antigenic variation and vaccine updates for the H9N2 AIV. Also, highlighted the critical functions of glycosylation in the influenza virus on the pathogenicity against mammals.
引用
收藏
页码:E659 / E670
页数:12
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