Structure of deformed wing virus, a major honey bee pathogen

J 2017

Structure of deformed wing virus, a major honey bee pathogen

ŠKUBNÍK, Karel, Jiří NOVÁČEK, Tibor FÜZIK, Antonin PRIDAL, Robert J. PAXTON et. al.

Basic information

Original name

Structure of deformed wing virus, a major honey bee pathogen

Authors

ŠKUBNÍK, Karel (203 Czech Republic, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Tibor FÜZIK (703 Slovakia, belonging to the institution), Antonin PRIDAL (203 Czech Republic), Robert J. PAXTON (276 Germany) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)

Edition

Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, National Academy of Sciences, 2017, 0027-8424

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 9.504

RIV identification code

RIV/00216224:14740/17:00096848

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1073/pnas.1615695114

UT WoS

000396893600075

Keywords in English

colony collapse disorder; virus; structure; Apis mellifera; honey bee

Abstract

V originále

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.

Links

LM2010005, research and development project

Name: Velká infrastruktura CESNET (Acronym: VI CESNET)

Investor: Ministry of Education, Youth and Sports of the CR

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

Citovat

ŠKUBNÍK, Karel, Jiří NOVÁČEK, Tibor FÜZIK, Antonin PRIDAL, Robert J. PAXTON and Pavel PLEVKA. Structure of deformed wing virus, a major honey bee pathogen. 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.

@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.

Detailed Information on Publication Record