N1 neuraminidase monoclonal antibodies 2H08 and 3H03 have decreased binding and inhibition properties against H1N1 influenza viruses circulating after 2018
- 1Icahn School of Medicine at Mount Sinai
Abstract
Influenza viruses are global public health problem. Vaccines are available but have to be updated annually due to antigenic drift of the main vaccine component, the surface glycoprotein hemagglutinin (HA). The second surface glycoprotein of the virus, neuraminidase (NA), has recently moved into the spotlight of vaccine development. However, its antigenic evolution is understudied. We found that two broadly protective N1 NA antibodies, which had previously been shown to bind and inhibit most N1 NA, lost activity to recent N1s from seasonal H1N1 viruses. Here, we show that this drop in activity can mostly be attributed to a change in electrostatic surface potential from neutral to positively charged. This effect was not observed when historic human plasma samples were tested, suggesting that the drop of activity is specific to the two tested mAbs but does not broadly impact the polyclonal human response. Finally, we confirmed that the tested mAbs were fully active against recently emerged pan-zootic clade 2.3.4.4b H5N1 NA.
Related
- Phenuivirus glycoprotein Gc domain is a conserved target of cross-functional monoclonal antibodies
- IgM monoclonal antibodies reduce IgG-mediated antibody-dependent enhancement of Zika and dengue virus infectivity
- A Panel of Human Monoclonal Antibodies for Tracking the Antigenic Evolution of Influenza H5N1 Clade 2.3.4.4b
- Structural analysis of the specificity of three neutralising human monoclonal antibodies against poliovirus
- DNA-Barcoded Polysaccharide Specific Monoclonal Antibodies Facilitate Sensitive and Multiplexed Detection of Cell Wall Polymers.
BibTeX
@misc{bhavsar2026neuraminidase,
title = {{N1 neuraminidase monoclonal antibodies 2H08 and 3H03 have decreased binding and inhibition properties against H1N1 influenza viruses circulating after 2018}},
author = {D. Bhavsar and E. Hermann and B. Monahan and J. Nardulli and C. Gleason and V. Simon and F. Krammer},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.26.761829},
url = {https://www.biorxiv.org/content/10.64898/2026.10.26.761829v1},
note = {CC BY-NC-ND},
}
RIS
TY - UNPB
TI - N1 neuraminidase monoclonal antibodies 2H08 and 3H03 have decreased binding and inhibition properties against H1N1 influenza viruses circulating after 2018
AU - D. Bhavsar
AU - E. Hermann
AU - B. Monahan
AU - J. Nardulli
AU - C. Gleason
AU - V. Simon
AU - F. Krammer
PY - 2026
DA - 2026/10/26
PB - bioRxiv
DO - 10.64898/2026.10.26.761829
UR - https://www.biorxiv.org/content/10.64898/2026.10.26.761829v1
AB - Influenza viruses are global public health problem. Vaccines are available but have to be updated annually due to antigenic drift of the main vaccine component, the surface glycoprotein hemagglutinin (HA). The second surface glycoprotein of the virus, neuraminidase (NA), has recently moved into the spotlight of vaccine development. However, its antigenic evolution is understudied. We found that two broadly protective N1 NA antibodies, which had previously been shown to bind and inhibit most N1 NA, lost activity to recent N1s from seasonal H1N1 viruses. Here, we show that this drop in activity can mostly be attributed to a change in electrostatic surface potential from neutral to positively charged. This effect was not observed when historic human plasma samples were tested, suggesting that the drop of activity is specific to the two tested mAbs but does not broadly impact the polyclonal human response. Finally, we confirmed that the tested mAbs were fully active against recently emerged pan-zootic clade 2.3.4.4b H5N1 NA.
ER -