The worldwide population of western honey bees (Apis mellifera) is under pressure from habitat loss, environmental stress, and pathogens, particularly viruses that cause lethal epidemics. Deformed wing virus (DWV) from the family Iflaviridae, together with its vector, the mite Varroa destructor, is likely the major threat to the world's honey bees. However, lack of knowledge of the atomic structures of iflaviruses has hindered the development of effective treatments against them. Here, we present the virion structures of DWV determined to a resolution of 3.1 Åusing cryo-electron microscopy and 3.8 Å by X-ray crystallography. The C-terminal extension of capsid protein VP3 folds into a globular protruding (P) domain, exposed on the virion surface. The P domain contains an Asp-His-Ser catalytic triad that is, together with five residues that are spatially close, conserved among iflaviruses. These residues may participate in receptor binding or provide the protease, lipase, or esterase activity required for entry of the virus into a host cell. Furthermore, nucleotides of the DWV RNA genome interact with VP3 subunits. The capsid protein residues involved in the RNA binding are conserved among honey bee iflaviruses, suggesting a putative role of the genome in stabilizing the virion or facilitating capsid assembly. Identifying the RNA-binding and putative catalytic sites within the DWV virion structure enables future analyses of how DWV and other iflaviruses infect insect cells and also opens up possibilities for the development of antiviral treatments.colony collapse disorder | virus | structure | Apis mellifera | honey bee

SignificanceHoney bee pollination is required to sustain the biodiversity of wild flora and for agricultural production; however, honey bee populations in Europe and North America are declining due to virus infections. Sacbrood virus (SBV) infection is lethal to honey bee larvae and decreases the fitness of honey bee colonies. Here we present the structure of the SBV particle and show that it contains 60 copies of a minor capsid protein attached to its surface. No similar minor capsid proteins have been previously observed in any of the related viruses. We also present a structural analysis of the genome release of SBV. The possibility of blocking virus genome delivery may provide a tool to prevent the spread of this honey bee pathogen.

Cryo-EM reveals the genome ejection mechanism of bacteriophage P68, a potential phage therapy agent against Staphylococcus aureus.