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@article{1381954,
author = {Škubník, Karel and Nováček, Jiří and Füzik, Tibor and Pridal, Antonin and Paxton, Robert J. and Plevka, Pavel},
article_location = {WASHINGTON},
article_number = {12},
doi = {http://dx.doi.org/10.1073/pnas.1615695114},
keywords = {colony collapse disorder; virus; structure; Apis mellifera; honey bee},
language = {eng},
issn = {0027-8424},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
title = {Structure of deformed wing virus, a major honey bee pathogen},
url = {http://www.pnas.org/content/pnas/114/12/3210.full.pdf},
volume = {114},
year = {2017}
}
TY - JOUR
ID - 1381954
AU - Škubník, Karel - Nováček, Jiří - Füzik, Tibor - Pridal, Antonin - Paxton, Robert J. - Plevka, Pavel
PY - 2017
TI - Structure of deformed wing virus, a major honey bee pathogen
JF - Proceedings of the National Academy of Sciences of the United States of America
VL - 114
IS - 12
SP - 3210-3215
EP - 3210-3215
PB - National Academy of Sciences
SN - 00278424
KW - colony collapse disorder
KW - virus
KW - structure
KW - Apis mellifera
KW - honey bee
UR - http://www.pnas.org/content/pnas/114/12/3210.full.pdf
L2 - http://www.pnas.org/content/pnas/114/12/3210.full.pdf
N2 - 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.
ER -
ŠKUBNÍK, Karel, Jiří NOVÁČEK, Tibor FÜZIK, Antonin PRIDAL, Robert J. PAXTON and Pavel PLEVKA. Structure of deformed wing virus, a major honey bee pathogen. \textit{Proceedings of the National Academy of Sciences of the United States of America}. WASHINGTON: National Academy of Sciences, 2017, vol.~114, No~12, p.~3210-3215. ISSN~0027-8424. Available from: https://dx.doi.org/10.1073/pnas.1615695114.
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