Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F16%3A43909689" target="_blank" >RIV/62156489:43210/16:43909689 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14740/16:00093718

Result on the web

<a href="http://dx.doi.org/10.1128/JVI.00680-16" target="_blank" >http://dx.doi.org/10.1128/JVI.00680-16</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1128/JVI.00680-16" target="_blank" >10.1128/JVI.00680-16</a>

Result language

angličtina

Original language name

Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution

Original language description

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 Å and 2.6 Å. 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 Å 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.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

—

Project

<a href="/en/project/LQ1601" target="_blank" >LQ1601: CEITEC 2020</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Virology

ISSN

0022-538X

e-ISSN

—

Volume of the periodical

90

Issue of the periodical within the volume

16

Country of publishing house

US - UNITED STATES

Number of pages

12

Pages from-to

7444-7455

UT code for WoS article

000382306500033

EID of the result in the Scopus database

2-s2.0-84982206764