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Virion structure of Iflavirus Slow bee paralysis virus at 2.6-Angstrom resolution

Kalynych, Sergei and Přidal, Antonín and Pálková, Lenka and Levdansky, Yevgen and Rodrigues De Miranda, Joachim and Plevka, Pavel (2016). Virion structure of Iflavirus Slow bee paralysis virus at 2.6-Angstrom resolution. Journal of virology. 90:16, 7444 –7455
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Official URL: http://dx.doi.org/10.1128/JVI.00680-16

Abstract

The western honeybee (Apis mellifera) is the most important commercial insect pollinator. However, bees are under pressure from habitat loss, environmental stress, and pathogens, including viruses that can cause lethal epidemics. Slow bee paralysis virus (SBPV) belongs to the Iflaviridae family of nonenveloped single-stranded RNA viruses. Here we present the structure of the SBPV virion determined from two crystal forms to resolutions of 3.4 angstrom and 2.6 angstrom. The overall structure of the virion resembles that of picornaviruses, with the three major capsid proteins VP1 to 3 organized into a pseudo-T3 icosahedral capsid. However, the SBPV capsid protein VP3 contains a C-terminal globular domain that has not been observed in other viruses from the order Picornavirales. The protruding (P) domains form "crowns" on the virion surface around each 5-fold axis in one of the crystal forms. However, the P domains are shifted 36 angstrom toward the 3-fold axis in the other crystal form. Furthermore, the P domain contains the Ser-His-Asp triad within a surface patch of eight conserved residues that constitutes a putative catalytic or receptor-binding site. The movements of the domain might be required for efficient substrate cleavage or receptor binding during virus cell entry. In addition, capsid protein VP2 contains an RGD sequence that is exposed on the virion surface, indicating that integrins might be cellular receptors of SBPV.IMPORTANCEPollination by honeybees is needed to sustain agricultural productivity as well as the biodiversity of wild flora. However, honey-bee populations in Europe and North America have been declining since the 1950s. Honeybee viruses from the Iflaviridae family are among the major causes of honeybee colony mortality. We determined the virion structure of an Iflavirus, slow bee paralysis virus (SBPV). SBPV exhibits unique structural features not observed in other picorna-like viruses. The SBPV capsid protein VP3 has a large C-terminal domain, five of which form highly prominent protruding "crowns" on the virion surface. However, the domains can change their positions depending on the conditions of the environment. The domain includes a putative catalytic or receptor binding site that might be important for SBPV cell entry.

Authors/Creators:Kalynych, Sergei and Přidal, Antonín and Pálková, Lenka and Levdansky, Yevgen and Rodrigues De Miranda, Joachim and Plevka, Pavel
Title:Virion structure of Iflavirus Slow bee paralysis virus at 2.6-Angstrom resolution
Series/Journal:Journal of virology (1098-5514)
Year of publishing :2016
Volume:90
Number:16
Page range:7444 –7455
Number of Pages:12
Publisher:American Society for Microbiology
Associated Programs and Other Stakeholders:SLU - Research Areas for the Future > Future Animal Health and Welfare
ISSN:1098-5514
Language:English
Publication Type:Journal article
Refereed:Yes
Article category:Scientific peer reviewed
Version:Accepted version
Full Text Status:Public
Agris subject categories.:L Animal production > L20 Animal ecology
L Animal production > L73 Animal diseases
Subjects:(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Structural Biology
(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology
(A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Cell Biology
Agrovoc terms:viruses, Apis mellifera
Keywords:colony collapse disorder, CCD, virus, Apis mellifera, honey bee, honeybee, bumblebee, Picornavirales, Iflaviridae, Iflavirus, picornavirus, virion, structure, X-ray, crystal, capsid, protein, jellyroll, inhibitor, antiviral, domain, catalytic site
URN:NBN:urn:nbn:se:slu:epsilon-e-3744
Permanent URL:
http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-e-3744
Additional ID:
Type of IDID
Web of Science (WoS)000382306500033
ID Code:13728
Faculty:NJ - Fakulteten för naturresurser och jordbruksvetenskap
Department:(NL, NJ) > Dept. of Ecology
(S) > Dept. of Ecology
Deposited By: SLUpub Connector
Deposited On:28 Oct 2016 08:26
Metadata Last Modified:28 Oct 2016 08:26

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