2018
Virion structure and genome delivery mechanism of sacbrood honeybee virus
PROCHÁZKOVÁ, Michaela, Tibor FÜZIK, Karel ŠKUBNÍK, Jana MORAVCOVÁ, Zorica UBIPARIP et. al.Základní údaje
Originální název
Virion structure and genome delivery mechanism of sacbrood honeybee virus
Autoři
PROCHÁZKOVÁ, Michaela (203 Česká republika, domácí), Tibor FÜZIK (703 Slovensko, domácí), Karel ŠKUBNÍK (203 Česká republika, domácí), Jana MORAVCOVÁ (203 Česká republika, domácí), Zorica UBIPARIP (688 Srbsko, domácí), A. PRIDAL (203 Česká republika) a Pavel PLEVKA (203 Česká republika, garant, domácí)
Vydání
Proceedings of the National Academy of Sciences of the United States of America, WASHINGTON, NATL ACAD SCIENCES, 2018, 0027-8424
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10607 Virology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 9.580
Kód RIV
RIV/00216224:14740/18:00106622
Organizační jednotka
Středoevropský technologický institut
UT WoS
000439574700056
Klíčová slova anglicky
honeybee; virus; structure; genome; release
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 23. 4. 2024 14:55, Mgr. Michal Petr
Anotace
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.
Návaznosti
LM2015043, projekt VaV |
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LQ1601, projekt VaV |
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3041, interní kód MU |
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335855, interní kód MU |
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