Figures
Influenza A virus particles containing both native and decoy glycoproteins
Confocal fluorescence microscopy image of influenza A virus particles displaying both native and decoy hemagglutinin (HA), the viral receptor-binding protein. Decoy HA is shown in green, while native HA is labeled with a stem-binding antibody (blue) and a head-binding antibody (purple). The decoy HA was introduced to modulate the effective surface density of HA and assess its impact on the binding of protective IgG antibodies. This study finds that bivalent antibody binding remains robust even at significantly reduced HA densities, highlighting how binding geometry and HA flexibility shape antibody avidity. Benegal et al. 2026
Image Credit: Ananya Benegal
Citation: (2026) PLoS Pathogens Issue Image | Vol. 22(2) April 2026. PLoS Pathog 22(2): ev22.i02. https://doi.org/10.1371/image.ppat.v22.i02
Published: April 14, 2026
Copyright: © 2026 . This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Confocal fluorescence microscopy image of influenza A virus particles displaying both native and decoy hemagglutinin (HA), the viral receptor-binding protein. Decoy HA is shown in green, while native HA is labeled with a stem-binding antibody (blue) and a head-binding antibody (purple). The decoy HA was introduced to modulate the effective surface density of HA and assess its impact on the binding of protective IgG antibodies. This study finds that bivalent antibody binding remains robust even at significantly reduced HA densities, highlighting how binding geometry and HA flexibility shape antibody avidity. Benegal et al. 2026
Image Credit: Ananya Benegal