Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus

Influenza A H9N2 virus causes economic loss to the poultry industry and has likely contributed to the genesis of H5N1 and H7N9 viruses. The neuraminidase (NA) of H9N2 virus, like haemagglutinin, is under antibody selective pressure and may undergo antigenic change; however, its antigenic structure r...

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Main Authors: Fei Wang, Jinsen Wu, Yajuan Wang, Zhimin Wan, Hongxia Shao, Kun Qian, Jianqiang Ye, Aijian Qin
Format: Article
Language:English
Published: Taylor & Francis Group 2021-01-01
Series:Emerging Microbes and Infections
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Online Access:https://www.tandfonline.com/doi/10.1080/22221751.2021.1879602
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author Fei Wang
Jinsen Wu
Yajuan Wang
Zhimin Wan
Hongxia Shao
Kun Qian
Jianqiang Ye
Aijian Qin
author_facet Fei Wang
Jinsen Wu
Yajuan Wang
Zhimin Wan
Hongxia Shao
Kun Qian
Jianqiang Ye
Aijian Qin
author_sort Fei Wang
collection DOAJ
description Influenza A H9N2 virus causes economic loss to the poultry industry and has likely contributed to the genesis of H5N1 and H7N9 viruses. The neuraminidase (NA) of H9N2 virus, like haemagglutinin, is under antibody selective pressure and may undergo antigenic change; however, its antigenic structure remains to be elucidated. In this study, we used monoclonal antibodies (mAbs) to probe the H9N2 viral NA residues that are key for antibody binding/inhibition. These mAbs fell into three groups based on their binding/inhibition of the NA of H9N2 viruses isolated during 1999–2019: group I only bounded the NA of the early 2000 H9N2 viruses but possessed no neutralizing ability, group II bounded and inhibited the NA of H9N2 viruses isolated before 2012, and group III reacted with most or all tested H9N2 viruses. We showed that NA residue 356 is key for the recognition by group I mAbs, residues 344, 368, 369, and 400 are key for the binding/inhibition of NA by group II antibodies, whereas residues 248, 253, and the 125/296 combination are key for neutralizing antibodies in group III. Our findings highlighted NA antigenic change of the circulating H9N2 viruses, and provided data for a more complete picture of the antigenic structure of H9N2 viral NA.
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spelling doaj-art-fbae79f6e68c48c7adb6f0ed854a5ec92025-08-20T01:50:45ZengTaylor & Francis GroupEmerging Microbes and Infections2222-17512021-01-0110121021910.1080/22221751.2021.1879602Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virusFei Wang0Jinsen Wu1Yajuan Wang2Zhimin Wan3Hongxia Shao4Kun Qian5Jianqiang Ye6Aijian Qin7Ministry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaMinistry of Education Key Lab for Avian Preventive Medicine, Yangzhou University, Jiangsu, People’s Republic of ChinaInfluenza A H9N2 virus causes economic loss to the poultry industry and has likely contributed to the genesis of H5N1 and H7N9 viruses. The neuraminidase (NA) of H9N2 virus, like haemagglutinin, is under antibody selective pressure and may undergo antigenic change; however, its antigenic structure remains to be elucidated. In this study, we used monoclonal antibodies (mAbs) to probe the H9N2 viral NA residues that are key for antibody binding/inhibition. These mAbs fell into three groups based on their binding/inhibition of the NA of H9N2 viruses isolated during 1999–2019: group I only bounded the NA of the early 2000 H9N2 viruses but possessed no neutralizing ability, group II bounded and inhibited the NA of H9N2 viruses isolated before 2012, and group III reacted with most or all tested H9N2 viruses. We showed that NA residue 356 is key for the recognition by group I mAbs, residues 344, 368, 369, and 400 are key for the binding/inhibition of NA by group II antibodies, whereas residues 248, 253, and the 125/296 combination are key for neutralizing antibodies in group III. Our findings highlighted NA antigenic change of the circulating H9N2 viruses, and provided data for a more complete picture of the antigenic structure of H9N2 viral NA.https://www.tandfonline.com/doi/10.1080/22221751.2021.1879602Influenza virusH9N2neuraminidasemonoclonal antibodieskey residuesantigenic change
spellingShingle Fei Wang
Jinsen Wu
Yajuan Wang
Zhimin Wan
Hongxia Shao
Kun Qian
Jianqiang Ye
Aijian Qin
Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
Emerging Microbes and Infections
Influenza virus
H9N2
neuraminidase
monoclonal antibodies
key residues
antigenic change
title Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
title_full Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
title_fullStr Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
title_full_unstemmed Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
title_short Identification of key residues involved in the neuraminidase antigenic variation of H9N2 influenza virus
title_sort identification of key residues involved in the neuraminidase antigenic variation of h9n2 influenza virus
topic Influenza virus
H9N2
neuraminidase
monoclonal antibodies
key residues
antigenic change
url https://www.tandfonline.com/doi/10.1080/22221751.2021.1879602
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