Detailed Information on Publication Record
2018
Virion structure and genome delivery mechanism of sacbrood honeybee virus
PROCHÁZKOVÁ, Michaela, Tibor FÜZIK, Karel ŠKUBNÍK, Jana MORAVCOVÁ, Zorica UBIPARIP et. al.Basic information
Original name
Virion structure and genome delivery mechanism of sacbrood honeybee virus
Authors
PROCHÁZKOVÁ, Michaela (203 Czech Republic, belonging to the institution), Tibor FÜZIK (703 Slovakia, belonging to the institution), Karel ŠKUBNÍK (203 Czech Republic, belonging to the institution), Jana MORAVCOVÁ (203 Czech Republic, belonging to the institution), Zorica UBIPARIP (688 Serbia, belonging to the institution), A. PRIDAL (203 Czech Republic) and Pavel PLEVKA (203 Czech Republic, guarantor, belonging to the institution)
Edition
Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, NATL ACAD SCIENCES, 2018, 0027-8424
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10607 Virology
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 9.580
RIV identification code
RIV/00216224:14740/18:00106622
Organization unit
Central European Institute of Technology
UT WoS
000439574700056
Keywords in English
honeybee; virus; structure; genome; release
Tags
International impact, Reviewed
Změněno: 23/4/2024 14:55, Mgr. Michal Petr
Abstract
V originále
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 angstrom and 12 angstrom 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.
Links
LM2015043, research and development project |
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LQ1601, research and development project |
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3041, interní kód MU |
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335855, interní kód MU |
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