Virion structure and genome delivery mechanism of sacbrood honeybee virus
| Autor: | T. Fuzik, Jana Moravcová, Antonín Přidal, K. Skubnik, Michaela Procházková, Zorica Ubiparip, Pavel Plevka |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
animal structures viruses POLIOVIRUS HUMAN RHINOVIRUS-14 virus Endosomes Genome Viral honeybee medicine.disease_cause CRYO-EM Crystallography X-Ray Genome release Endosome membrane Virus BEE PARALYSIS VIRUS 03 medical and health sciences ANTIVIRAL AGENTS medicine Animals RNA Viruses structure genome 3-DIMENSIONAL STRUCTURE Multidisciplinary biology CLEAVAGE Poliovirus fungi Virion Biology and Life Sciences food and beverages Honey bee Biological Sciences Bees biology.organism_classification Virology 3. Good health Biophysics and Computational Biology 030104 developmental biology Capsid RESOLUTION Iflaviridae ENTRY HUMAN ENTEROVIRUS 71 behavior and behavior mechanisms Picornavirales Capsid Proteins |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | Significance Honey bee pollination is required to sustain the biodiversity of wild flora and for agricultural production; however, honey bee populations in Europe and North America are declining due to virus infections. Sacbrood virus (SBV) infection is lethal to honey bee larvae and decreases the fitness of honey bee colonies. Here we present the structure of the SBV particle and show that it contains 60 copies of a minor capsid protein attached to its surface. No similar minor capsid proteins have been previously observed in any of the related viruses. We also present a structural analysis of the genome release of SBV. The possibility of blocking virus genome delivery may provide a tool to prevent the spread of this honey bee pathogen. 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. |
| Databáze: | OpenAIRE |
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