Detailed Information on Publication Record
2017
Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen
SPURNÝ, Radovan, Antonin PRIDAL, Lenka PÁLKOVÁ, Hoa Khanh TRAN KIEM, Joachim R. DE MIRANDA et. al.Basic information
Original name
Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen
Authors
SPURNÝ, Radovan (703 Slovakia, belonging to the institution), Antonin PRIDAL (203 Czech Republic), Lenka PÁLKOVÁ (203 Czech Republic, belonging to the institution), Hoa Khanh TRAN KIEM (704 Viet Nam, belonging to the institution), Joachim R. DE MIRANDA (752 Sweden) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)
Edition
JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2017, 0022-538X
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:
Impact factor
Impact factor: 4.368
RIV identification code
RIV/00216224:14740/17:00096847
Organization unit
Central European Institute of Technology
UT WoS
000398098300016
Keywords in English
virus; Apis mellifera; honey bee; honeybee; Picornavirales; Dicistroviridae; Cripavirus; Triatovirus; virion; structure; X ray; crystallography; capsid; insect disease; X-ray crystallography
Tags
International impact, Reviewed
Změněno: 27/2/2018 16:54, Mgr. Pavla Foltynová, Ph.D.
Abstract
V originále
Viral diseases are a major threat to honeybee (Apis mellifera) populations worldwide and therefore an important factor in reliable crop pollination and food security. Black queen cell virus (BQCV) is the etiological agent of a fatal disease of honeybee queen larvae and pupae. The virus belongs to the genus Triatovirus from the family Dicistroviridae, which is part of the order Picornavirales. Here we present a crystal structure of BQCV determined to a resolution of 3.4 angstrom. The virion is formed by 60 copies of each of the major capsid proteins VP1, VP2, and VP3; however, there is no density corresponding to a 75-residue-long minor capsid protein VP4 encoded by the BQCV genome. We show that the VP4 subunits are present in the crystallized virions that are infectious. This aspect of the BQCV virion is similar to that of the previously characterized triatoma virus and supports the recent establishment of the separate genus Triatovirus within the family Dicistroviridae. The C terminus of VP1 and CD loops of capsid proteins VP1 and VP3 of BQCV form 34-angstrom-tall finger-like protrusions at the virion surface. The protrusions are larger than those of related dicistroviruses. IMPORTANCE The western honeybee is the most important pollinator of all, and it is required to sustain the agricultural production and biodiversity of wild flowering plants. However, honeybee populations worldwide are suffering from virus infections that cause colony losses. One of the most common, and least known, honeybee pathogens is black queen cell virus (BQCV), which at high titers causes queen larvae and pupae to turn black and die. Here we present the three-dimensional virion structure of BQCV, determined by X-ray crystallography. The structure of BQCV reveals large protrusions on the virion surface. Capsid protein VP1 of BQCV does not contain a hydrophobic pocket. Therefore, the BQCV virion structure provides evidence that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.
Links
| LM2010005, research and development project |
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| LM2015043, research and development project |
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| LQ1601, research and development project |
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