J 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

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
Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
LQ1601, research and development project
Name: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR
3041, interní kód MU
Name: Structural studies of human and animal pathogens from the order Picornavirales
Investor: EMBO (European Molecular Biology Organization)
335855, interní kód MU
Name: Structural studies of human picornaviruses directed towards development of anti-viral compounds (Acronym: PicoDrugs)
Investor: European Union, Ideas