دورية أكاديمية
Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen.
العنوان: | Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen. |
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المؤلفون: | Spurny R; Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic., Přidal A; Department of Zoology, Fishery, Hydrobiology, and Apidology, Faculty of Agronomy, Mendel University in Brno, Brno, Czech Republic., Pálková L; Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic., Kiem HKT; Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic., de Miranda JR; Department of Ecology, Swedish University of Agricultural Sciences, Uppsala, Sweden., Plevka P; Structural Virology, Central European Institute of Technology, Masaryk University, Brno, Czech Republic pavel.plevka@ceitec.muni.cz. |
المصدر: | Journal of virology [J Virol] 2017 Feb 28; Vol. 91 (6). Date of Electronic Publication: 2017 Feb 28 (Print Publication: 2017). |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0113724 Publication Model: Electronic-Print Cited Medium: Internet ISSN: 1098-5514 (Electronic) Linking ISSN: 0022538X NLM ISO Abbreviation: J Virol Subsets: MEDLINE |
أسماء مطبوعة: | Publication: Washington Dc : American Society For Microbiology Original Publication: Baltimore, American Society for Microbiology. |
مواضيع طبية MeSH: | Dicistroviridae/*ultrastructure , Virion/*ultrastructure, Animals ; Bees/virology ; Capsid Proteins/chemistry ; Crystallography, X-Ray ; Models, Molecular ; Protein Conformation ; Viral Structures |
مستخلص: | 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 Å. 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-Å-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. (Copyright © 2017 Spurny et al.) |
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فهرسة مساهمة: | Keywords: Apis mellifera; Cripavirus; Dicistroviridae; Picornavirales; Triatovirus; X ray; X-ray crystallography; capsid; crystallography; honey bee; honeybee; insect disease; structure; virion; virus |
المشرفين على المادة: | 0 (Capsid Proteins) |
تواريخ الأحداث: | Date Created: 20170113 Date Completed: 20170518 Latest Revision: 20190329 |
رمز التحديث: | 20231215 |
مُعرف محوري في PubMed: | PMC5331821 |
DOI: | 10.1128/JVI.02100-16 |
PMID: | 28077635 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1098-5514 |
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DOI: | 10.1128/JVI.02100-16 |