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A Single Amino Acid at Position 158 in Hemagglutinin Affects the Antigenic Property of Eurasian Avian-like H1N1 Swine Influenza Viruses
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  • Zeng Wang,
  • Yan Chen,
  • Huayuan Chen,
  • Fei Meng,
  • Shiyu Tao,
  • Shujie Ma,
  • Chuanling Qiao,
  • Hualan Chen,
  • huanliang yang
Zeng Wang
College of Veterinary Medicine Henan Agricultural University Zhengzhou People's Republic of China
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Yan Chen
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Huayuan Chen
College of Veterinary Medicine Henan Agricultural University Zhengzhou People's Republic of China
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Fei Meng
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Shiyu Tao
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Shujie Ma
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Chuanling Qiao
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Hualan Chen
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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huanliang yang
State Key Laboratory of Veterinary Biotechnology Harbin Veterinary Research Institute Chinese Academy of Agricultural Sciences (CAAS) Harbin People's Republic of China
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Abstract

Influenza viruses have been posing a great threat to public health and animal industry. The developed vaccines have been widely used to reduce the risk of potential pandemic; however, the ongoing antigenic drift makes influenza virus escape from host immune response and hampers vaccine efficacy. Until now, the genetic basis of antigenic variation remains largely unknown. In this study, we used A/swine/Guangxi/18/2011 (GX/18) and A/swine/Guangdong/104/2013 (GD/104) as models to explore the molecular determinant for antigenic variation of Eurasian avian-like H1N1 (EA H1N1) swine influenza viruses (SIVs), and found that the GD/104 virus exhibited 32~64-fold lower antigenic cross-reactivity with antibodies against GX/18 virus. Therefore, we generated polyclonal antibodies against GX/18 or GD/104 virus and a monoclonal antibody (mAb), named mAb102-95, targeted to the hemagglutinin (HA) protein of GX/18 virus, and found that a single amino acid substitution at position 158 in HA protein substantially altered the antigenicity of virus. The reactivity of GX/18 virus containing G158E mutation with the mAb102-95 decreased 8-fold than that of the parental strain. Contrarily, the reactivity of GD/104 virus bearing E158G mutation with the mAb102-95 increased by 32 times as compared with that of the parental virus. Structural analysis showed that the amino acid mutation from G to E was accompanied with the R group changing from -H to -(CH 2) 2-COOH. The induced steric effect and increased hydrophilicity of HA protein surface jointly contributed to the antigenic drift of EA H1N1 SIVs. Our study provides experimental evidence that G158E mutation in HA protein affects the antigenic property of EA H1N1 SIVs, and widens our horizon on the antigenic drift of influenza virus.

Peer review status:UNDER REVIEW

21 May 2021Submitted to Transboundary and Emerging Diseases
21 May 2021Assigned to Editor
21 May 2021Submission Checks Completed
26 May 2021Reviewer(s) Assigned