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Abstract
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.
Keywords
honeybee, virus, structure, genome, release, BEE PARALYSIS VIRUS, HUMAN ENTEROVIRUS 71, 3-DIMENSIONAL STRUCTURE, HUMAN RHINOVIRUS-14, ANTIVIRAL AGENTS, CRYO-EM, POLIOVIRUS, RESOLUTION, CLEAVAGE, ENTRY

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Chicago
Procházková, Michaela, Tibor Füzik, Karel Škubník, Jana Moravcová, Zorica Ubiparip, Antonín Přidal, and Pavel Plevka. 2018. “Virion Structure and Genome Delivery Mechanism of Sacbrood Honeybee Virus.” Proceedings of the National Academy of Sciences of the United States of America 115 (30): 7759–7764.
APA
Procházková, M., Füzik, T., Škubník, K., Moravcová, J., Ubiparip, Z., Přidal, A., & Plevka, P. (2018). Virion structure and genome delivery mechanism of sacbrood honeybee virus. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 115(30), 7759–7764.
Vancouver
1.
Procházková M, Füzik T, Škubník K, Moravcová J, Ubiparip Z, Přidal A, et al. Virion structure and genome delivery mechanism of sacbrood honeybee virus. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2018;115(30):7759–64.
MLA
Procházková, Michaela et al. “Virion Structure and Genome Delivery Mechanism of Sacbrood Honeybee Virus.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 115.30 (2018): 7759–7764. Print.
@article{8587488,
  abstract     = {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.},
  author       = {Proch{\'a}zkov{\'a}, Michaela and F{\"u}zik, Tibor and \v{S}kubn{\'i}k, Karel and Moravcov{\'a}, Jana and Ubiparip, Zorica and P\v{r}idal, Anton{\'i}n and Plevka, Pavel},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  language     = {eng},
  number       = {30},
  pages        = {7759--7764},
  title        = {Virion structure and genome delivery mechanism of sacbrood honeybee virus},
  url          = {http://dx.doi.org/10.1073/pnas.1722018115},
  volume       = {115},
  year         = {2018},
}

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