Virion Structure and In Vitro Genome Release Mechanism of
Dicistrovirus Kashmir Bee Virus

J 2021

Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus

MUKHAMEDOVA, Liya, Tibor FÜZIK, Jiří NOVÁČEK, Dominik HREBÍK, A. PRIDAL et. al.

Basic information

Original name

Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus

Authors

MUKHAMEDOVA, Liya (643 Russian Federation, belonging to the institution), Tibor FÜZIK (703 Slovakia, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Dominik HREBÍK (703 Slovakia, belonging to the institution), A. PRIDAL, G.A. MARTI, D.M.A. GUERIN and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)

Edition

Journal of Virology, WASHINGTON, American Society for Microbiology, 2021, 0022-538X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10607 Virology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.549

RIV identification code

RIV/00216224:14740/21:00119637

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1128/JVI.01950-20

UT WoS

000652658800002

Keywords in English

RNA; capsid opening; genome release; iflavirus

Abstract

V originále

Infections with Kashmir bee virus (KBV) are lethal for honeybees and have been associated with colony collapse disorder. KBV and closely related viruses contribute to the ongoing decline in the number of honeybee colonies in North America, Europe, Australia, and other parts of the world. Despite the economic and ecological impact of KBV, its structure and infection process remain unknown. Here, we present the structure of the virion of KBV determined to a resolution of 2.8 angstrom. We show that the exposure of KBV to acidic pH induces a reduction in interpentamer contacts within capsids and the reorganization of its RNA genome from a uniform distribution to regions of high and low density. Capsids of KBV crack into pieces at acidic pH, resulting in the formation of open particles lacking pentamers of capsid proteins. The large openings of capsids enable the rapid release of genomes and thus limit the probability of their degradation by RNases. The opening of capsids may be a shared mechanism for the genome release of viruses from the family Dicistroviridae. IMPORTANCE The western honeybee (Apis mellifera) is indispensable for maintaining agricultural productivity as well as the abundance and diversity of wild flowering plants. However, bees suffer from environmental pollution, parasites, and pathogens, including viruses. Outbreaks of virus infections cause the deaths of individual honeybees as well as collapses of whole colonies. Kashmir bee virus has been associated with colony collapse disorder in the United States, and no cure for the disease is currently available. Here, we report the structure of an infectious particle of Kashmir bee virus and show how its protein capsid opens to release the genome. Our structural characterization of the infection process determined that therapeutic compounds stabilizing contacts between pentamers of capsid proteins could prevent the genome release of the virus.

Links

GX19-25982X, research and development project

Name: Analýza replikace enterovirů s využitím elektronové mikroskopie

Investor: Czech Science Foundation

LM2018127, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)

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

90127, large research infrastructures

Name: CIISB II

Citovat

MUKHAMEDOVA, Liya, Tibor FÜZIK, Jiří NOVÁČEK, Dominik HREBÍK, A. PRIDAL, G.A. MARTI, D.M.A. GUERIN and Pavel PLEVKA. Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus. Journal of Virology. WASHINGTON: American Society for Microbiology, 2021, vol. 95, No 11, p. nestrankovano, 11 pp. ISSN 0022-538X. Available from: https://dx.doi.org/10.1128/JVI.01950-20.

@article{1832006,
   author = {Mukhamedova, Liya and Füzik, Tibor and Nováček, Jiří and Hrebík, Dominik and Pridal, A. and Marti, G.A. and Guerin, D.M.A. and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {11},
   doi = {http://dx.doi.org/10.1128/JVI.01950-20},
   keywords = {RNA; capsid opening; genome release; iflavirus},
   language = {eng},
   issn = {0022-538X},
   journal = {Journal of Virology},
   title = {Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus},
   url = {https://journals.asm.org/doi/10.1128/JVI.01950-20},
   volume = {95},
   year = {2021}
}

TY  - JOUR
ID  - 1832006
AU  - Mukhamedova, Liya - Füzik, Tibor - Nováček, Jiří - Hrebík, Dominik - Pridal, A. - Marti, G.A. - Guerin, D.M.A. - Plevka, Pavel
PY  - 2021
TI  - Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus
JF  - Journal of Virology
VL  - 95
IS  - 11
SP  - nestrankovano
EP  - nestrankovano
PB  - American Society for Microbiology
SN  - 0022538X
KW  - RNA
KW  - capsid opening
KW  - genome release
KW  - iflavirus
UR  - https://journals.asm.org/doi/10.1128/JVI.01950-20
N2  - Infections with Kashmir bee virus (KBV) are lethal for honeybees and have been associated with colony collapse disorder. KBV and closely related viruses contribute to the ongoing decline in the number of honeybee colonies in North America, Europe, Australia, and other parts of the world. Despite the economic and ecological impact of KBV, its structure and infection process remain unknown. Here, we present the structure of the virion of KBV determined to a resolution of 2.8 angstrom. We show that the exposure of KBV to acidic pH induces a reduction in interpentamer contacts within capsids and the reorganization of its RNA genome from a uniform distribution to regions of high and low density. Capsids of KBV crack into pieces at acidic pH, resulting in the formation of open particles lacking pentamers of capsid proteins. The large openings of capsids enable the rapid release of genomes and thus limit the probability of their degradation by RNases. The opening of capsids may be a shared mechanism for the genome release of viruses from the family Dicistroviridae. IMPORTANCE The western honeybee (Apis mellifera) is indispensable for maintaining agricultural productivity as well as the abundance and diversity of wild flowering plants. However, bees suffer from environmental pollution, parasites, and pathogens, including viruses. Outbreaks of virus infections cause the deaths of individual honeybees as well as collapses of whole colonies. Kashmir bee virus has been associated with colony collapse disorder in the United States, and no cure for the disease is currently available. Here, we report the structure of an infectious particle of Kashmir bee virus and show how its protein capsid opens to release the genome. Our structural characterization of the infection process determined that therapeutic compounds stabilizing contacts between pentamers of capsid proteins could prevent the genome release of the virus.
ER  -

MUKHAMEDOVA, Liya, Tibor FÜZIK, Jiří NOVÁČEK, Dominik HREBÍK, A. PRIDAL, G.A. MARTI, D.M.A. GUERIN and Pavel PLEVKA. Virion Structure and In Vitro Genome Release Mechanism of Dicistrovirus Kashmir Bee Virus. \textit{Journal of Virology}. WASHINGTON: American Society for Microbiology, 2021, vol.~95, No~11, p.~nestrankovano, 11 pp. ISSN~0022-538X. Available from: https://dx.doi.org/10.1128/JVI.01950-20.

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