Key result
High-resolution cryo-electron microscopy revealed the 2.8-Angstrom structure of Human Parechovirus 3 in complex with a neutralizing antibody Fab, defining the epitope that prevents cell binding.
Why the study?
Human parechovirus 3 is a prevalent cause of sepsis-like symptoms in neonates lacking effective treatments, creating an urgent need for structural and molecular insights into virus neutralization.
The high-resolution structure of HPeV3 with a neutralizing antibody defines the binding epitope, providing insights for potential treatments for HPeV3-induced sepsis-like symptoms in neonates.
Human parechovirus 3 (HPeV3) is receiving increasing attention as a prevalent cause of sepsis-like symptoms in neonates, for which, despite the severity of disease, there are no effective treatments available. Structural and molecular insights into virus neutralization are urgently needed, especially as clinical cases are on the rise. Toward this goal, we present the first structure of HPeV3 in complex with fragments from a neutralizing monoclonal antibody. At high resolution, it was possible to precisely define the epitope that, when targeted, prevents virions from binding to cells. Such an atomic-level description is useful for understanding host-pathogen interactions and viral pathogenesis mechanisms and for finding potential cures for infection and disease.
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Domanska et al. (2018) studied Human parechovirus 3 (HPeV3) infection. Cryo-Electron Microscopy of HPeV3 in complex with Fab from a neutralizing antibody was evaluated on Atomic-level structure and epitope definition. High-resolution cryo-electron microscopy revealed the 2.8-Angstrom structure of Human Parechovirus 3 in complex with a neutralizing antibody Fab, defining the epitope that prevents cell binding.
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