Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases

Influenza A viruses (IAVs) continue to pose a huge threat to public health, and their prevention and treatment remain major international issues. Neuraminidase (NA) is the second most abundant surface glycoprotein on influenza viruses, and antibodies to NA have been shown to be effective against inf...

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Bibliographic Details
Published in:PloS one 2024-05, Vol.19 (5), p.e0302865-e0302865
Main Authors: Chen, Nan, Wang, Renxi, Zhu, Wanlu, Hao, Xiangjun, Wang, Jing, Chen, Guojiang, Qiao, ChunXia, Li, Xinying, Liu, Chenghua, Shen, Beifen, Feng, Jiannan, Chai, Lihui, Yu, Zuyin, Xiao, He
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antibodies, Monoclonal - immunology
Antibodies, Viral - immunology
Antiviral activity
Antiviral agents
Antiviral Agents - pharmacology
Avian flu
Avian influenza
Avian influenza viruses
Biology and life sciences
Control
Exo-a-sialidase
Glycoproteins
Health aspects
Humans
Infection
Infections
Influenza
Influenza A
Influenza A Virus, H1N1 Subtype - immunology
Influenza A Virus, H3N2 Subtype - immunology
Influenza A Virus, H5N1 Subtype - immunology
Influenza A Virus, H7N9 Subtype - immunology
Influenza viruses
Medical research
Medicine and health sciences
Medicine, Experimental
Mice
Mice, Inbred BALB C
Monoclonal antibodies
Neuraminidase - antagonists & inhibitors
Neuraminidase - immunology
Neuraminidase - metabolism
Physiological aspects
Plasmids
Polyethylene glycol
Protein binding
Proteins
Public health
Research and Analysis Methods
Scientific equipment and supplies industry
Testing
Viral antibodies
Viral infections
Viral Proteins - immunology
Viral Proteins - metabolism
Viruses
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Summary:Influenza A viruses (IAVs) continue to pose a huge threat to public health, and their prevention and treatment remain major international issues. Neuraminidase (NA) is the second most abundant surface glycoprotein on influenza viruses, and antibodies to NA have been shown to be effective against influenza infection. In this study, we generated a monoclonal antibody (mAb), named FNA1, directed toward N1 NAs. FNA1 reacted with H1N1 and H5N1 NA, but failed to react with the NA proteins of H3N2 and H7N9. In vitro, FNA1 displayed potent antiviral activity that mediated both NA inhibition (NI) and blocking of pseudovirus release. Moreover, residues 219, 254, 358, and 388 in the NA protein were critical for FNA1 binding to H1N1 NA. However, further validation is necessary to confirm whether FNA1 mAb is indeed a good inhibitor against NA for application against H1N1 and H5N1 viruses.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0302865