Virion structure and genome delivery mechanism of sacbrood honeybee virus
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F18%3A43913742" target="_blank" >RIV/62156489:43210/18:43913742 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14740/18:00106622
Result on the web
<a href="https://doi.org/10.1073/pnas.1722018115" target="_blank" >https://doi.org/10.1073/pnas.1722018115</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.1722018115" target="_blank" >10.1073/pnas.1722018115</a>
Alternative languages
Result language
angličtina
Original language name
Virion structure and genome delivery mechanism of sacbrood honeybee virus
Original language description
Infection by sacbrood virus (SBV) from the family Iflaviridae is lethal to honey bee larvae but only rarely causes the collapse of honey bee colonies. Despite the negative effect of SBV on honey bees, the structure of its particles and mechanism of its genome delivery are unknown. Here we present the crystal structure of SBV virion and show that it contains 60 copies of a minor capsid protein (MiCP) attached to the virion surface. No similar MiCPs have been previously reported in any of the related viruses from the order Picornavirales. The location of the MiCP coding sequence within the SBV genome indicates that the MiCP evolved from a C-terminal extension of a major capsid protein by the introduction of a cleavage site for a virus protease. The exposure of SBV to acidic pH, which the virus likely encounters during cell entry, induces the formation of pores at threefold and fivefold axes of the capsid that are 7 Å and 12 Å in diameter, respectively. This is in contrast to vertebrate picornaviruses, in which the pores along twofold icosahedral symmetry axes are currently considered the most likely sites for genome release. SBV virions lack VP4 subunits that facilitate the genome delivery of many related dicistroviruses and picornaviruses. MiCP subunits induce liposome disruption in vitro, indicating that they are functional analogs of VP4 subunits and enable the virus genome to escape across the endosome membrane into the cell cytoplasm.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10607 - Virology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the United States of America
ISSN
0027-8424
e-ISSN
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Volume of the periodical
115
Issue of the periodical within the volume
30
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
7759-7764
UT code for WoS article
000439574700056
EID of the result in the Scopus database
2-s2.0-85052022569