tetano
Editor, Senior Moderator
PLoS One
. 2024 May 9;19(5):e0302865.
doi: 10.1371/journal.pone.0302865. eCollection 2024. Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases
Nan Chen[SUP] 1 [/SUP], Renxi Wang[SUP] 2 [/SUP], Wanlu Zhu[SUP] 1 3 [/SUP], Xiangjun Hao[SUP] 1 3 [/SUP], Jing Wang[SUP] 1 [/SUP], Guojiang Chen[SUP] 1 [/SUP], ChunXia Qiao[SUP] 1 [/SUP], Xinying Li[SUP] 1 [/SUP], Chenghua Liu[SUP] 1 [/SUP], Beifen Shen[SUP] 1 [/SUP], Jiannan Feng[SUP] 1 [/SUP], Lihui Chai[SUP] 3 [/SUP], Zuyin Yu[SUP] 4 [/SUP], He Xiao[SUP] 1 [/SUP]
Affiliations
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.
. 2024 May 9;19(5):e0302865.
doi: 10.1371/journal.pone.0302865. eCollection 2024. Development and characterization of an antibody that recognizes influenza virus N1 neuraminidases
Nan Chen[SUP] 1 [/SUP], Renxi Wang[SUP] 2 [/SUP], Wanlu Zhu[SUP] 1 3 [/SUP], Xiangjun Hao[SUP] 1 3 [/SUP], Jing Wang[SUP] 1 [/SUP], Guojiang Chen[SUP] 1 [/SUP], ChunXia Qiao[SUP] 1 [/SUP], Xinying Li[SUP] 1 [/SUP], Chenghua Liu[SUP] 1 [/SUP], Beifen Shen[SUP] 1 [/SUP], Jiannan Feng[SUP] 1 [/SUP], Lihui Chai[SUP] 3 [/SUP], Zuyin Yu[SUP] 4 [/SUP], He Xiao[SUP] 1 [/SUP]
Affiliations
- PMID: 38723016
- DOI: 10.1371/journal.pone.0302865
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.