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Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses

Arne Matthys (UGent) , Jan Félix (UGent) , João Portela Catani (UGent) , Kenny Roose (UGent) , Wim Nerinckx (UGent) , Benthe Van Buyten (UGent) , Daria Fijalkowska (UGent) , Nico Callewaert (UGent) , Savvas Savvides (UGent) and Xavier Saelens (UGent)
(2025) NATURE COMMUNICATIONS. 16(1).
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Abstract
Influenza B viruses are antigenically diverse and contribute significantly to the annual influenza burden. Here we report influenza B virus neutralizing single-domain antibodies that target highly conserved regions of the hemagglutinin and neuraminidase. Structural studies by single particle electron cryo-microscopy (cryo-EM) revealed that one of these single-domain antibodies prevents the conformational transition of the viral hemagglutinin to the post-fusion state by targeting a quaternary epitope spanning two protomers in the hemagglutinin-stem region. A second single-domain antibody broadly inhibits influenza B neuraminidase activity, including an oseltamivir-resistant neuraminidase, and its complex with neuraminidase elucidated by single particle cryo-EM established that it binds to residues in the neuraminidase catalytic site. Head-to-tail fusions of these single-domain antibodies led to bispecific binders that further improved the neutralization breadth and potency against influenza B viruses. These single-domain antibodies, fused to a human IgG1-Fc domain, fully protected female mice against an otherwise lethal influenza B virus challenge. Our findings underscore the potential of engineered single-domain antibodies to help control influenza B virus infections.
Keywords
CRYO-EM, MEMBRANE, ORIENTATION, EPITOPES, COSTS

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MLA
Matthys, Arne, et al. “Single-Domain Antibodies Directed against Hemagglutinin and Neuraminidase Protect against Influenza B Viruses.” NATURE COMMUNICATIONS, vol. 16, no. 1, 2025, doi:10.1038/s41467-025-60232-3.
APA
Matthys, A., Félix, J., Portela Catani, J., Roose, K., Nerinckx, W., Van Buyten, B., … Saelens, X. (2025). Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses. NATURE COMMUNICATIONS, 16(1). https://doi.org/10.1038/s41467-025-60232-3
Chicago author-date
Matthys, Arne, Jan Félix, João Portela Catani, Kenny Roose, Wim Nerinckx, Benthe Van Buyten, Daria Fijalkowska, Nico Callewaert, Savvas Savvides, and Xavier Saelens. 2025. “Single-Domain Antibodies Directed against Hemagglutinin and Neuraminidase Protect against Influenza B Viruses.” NATURE COMMUNICATIONS 16 (1). https://doi.org/10.1038/s41467-025-60232-3.
Chicago author-date (all authors)
Matthys, Arne, Jan Félix, João Portela Catani, Kenny Roose, Wim Nerinckx, Benthe Van Buyten, Daria Fijalkowska, Nico Callewaert, Savvas Savvides, and Xavier Saelens. 2025. “Single-Domain Antibodies Directed against Hemagglutinin and Neuraminidase Protect against Influenza B Viruses.” NATURE COMMUNICATIONS 16 (1). doi:10.1038/s41467-025-60232-3.
Vancouver
1.
Matthys A, Félix J, Portela Catani J, Roose K, Nerinckx W, Van Buyten B, et al. Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses. NATURE COMMUNICATIONS. 2025;16(1).
IEEE
[1]
A. Matthys et al., “Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses,” NATURE COMMUNICATIONS, vol. 16, no. 1, 2025.
@article{01K0XNRF495K59CCVX3778H6N0,
  abstract     = {{Influenza B viruses are antigenically diverse and contribute significantly to the annual influenza burden. Here we report influenza B virus neutralizing single-domain antibodies that target highly conserved regions of the hemagglutinin and neuraminidase. Structural studies by single particle electron cryo-microscopy (cryo-EM) revealed that one of these single-domain antibodies prevents the conformational transition of the viral hemagglutinin to the post-fusion state by targeting a quaternary epitope spanning two protomers in the hemagglutinin-stem region. A second single-domain antibody broadly inhibits influenza B neuraminidase activity, including an oseltamivir-resistant neuraminidase, and its complex with neuraminidase elucidated by single particle cryo-EM established that it binds to residues in the neuraminidase catalytic site. Head-to-tail fusions of these single-domain antibodies led to bispecific binders that further improved the neutralization breadth and potency against influenza B viruses. These single-domain antibodies, fused to a human IgG1-Fc domain, fully protected female mice against an otherwise lethal influenza B virus challenge. Our findings underscore the potential of engineered single-domain antibodies to help control influenza B virus infections.}},
  articleno    = {{5831}},
  author       = {{Matthys, Arne and Félix, Jan and Portela Catani, João and Roose, Kenny and Nerinckx, Wim and Van Buyten, Benthe and Fijalkowska, Daria and Callewaert, Nico and Savvides, Savvas and Saelens, Xavier}},
  issn         = {{2041-1723}},
  journal      = {{NATURE COMMUNICATIONS}},
  keywords     = {{CRYO-EM,MEMBRANE,ORIENTATION,EPITOPES,COSTS}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{19}},
  title        = {{Single-domain antibodies directed against hemagglutinin and neuraminidase protect against influenza B viruses}},
  url          = {{http://doi.org/10.1038/s41467-025-60232-3}},
  volume       = {{16}},
  year         = {{2025}},
}
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