Structure of deformed wing virus, a major honey bee pathogen

Warning

This publication doesn't include Faculty of Arts. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

ŠKUBNÍK Karel NOVÁČEK Jiří FÜZIK Tibor PRIDAL Antonin PAXTON Robert J. PLEVKA Pavel

Year of publication 2017
Type Article in Periodical
Magazine / Source Proceedings of the National Academy of Sciences of the United States of America
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://www.pnas.org/content/pnas/114/12/3210.full.pdf
Doi http://dx.doi.org/10.1073/pnas.1615695114
Field Microbiology, virology
Keywords colony collapse disorder; virus; structure; Apis mellifera; honey bee
Description 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 angstrom using cryo-electron microscopy and 3.8 angstrom 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.