5LK8
single particle reconstruction of slow bee paralysis virus empty particle
5LK8 の概要
エントリーDOI | 10.2210/pdb5lk8/pdb |
EMDBエントリー | 4064 |
分子名称 | VP1, VP2, VP3 (3 entities in total) |
機能のキーワード | icosahedral virus, honebee virus, iflavirus, virus |
由来する生物種 | Slow bee paralysis virus 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 107755.33 |
構造登録者 | |
主引用文献 | Kalynych, S.,Fuzik, T.,Pridal, A.,de Miranda, J.,Plevka, P. Cryo-EM study of slow bee paralysis virus at low pH reveals iflavirus genome release mechanism. Proc. Natl. Acad. Sci. U.S.A., 114:598-603, 2017 Cited by PubMed Abstract: Viruses from the family Iflaviridae are insect pathogens. Many of them, including slow bee paralysis virus (SBPV), cause lethal diseases in honeybees and bumblebees, resulting in agricultural losses. Iflaviruses have nonenveloped icosahedral virions containing single-stranded RNA genomes. However, their genome release mechanism is unknown. Here, we show that low pH promotes SBPV genome release, indicating that the virus may use endosomes to enter host cells. We used cryo-EM to study a heterogeneous population of SBPV virions at pH 5.5. We determined the structures of SBPV particles before and after genome release to resolutions of 3.3 and 3.4 Å, respectively. The capsids of SBPV virions in low pH are not expanded. Thus, SBPV does not appear to form "altered" particles with pores in their capsids before genome release, as is the case in many related picornaviruses. The egress of the genome from SBPV virions is associated with a loss of interpentamer contacts mediated by N-terminal arms of VP2 capsid proteins, which result in the expansion of the capsid. Pores that are 7 Å in diameter form around icosahedral threefold symmetry axes. We speculate that they serve as channels for the genome release. Our findings provide an atomic-level characterization of the genome release mechanism of iflaviruses. PubMed: 28053231DOI: 10.1073/pnas.1616562114 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.42 Å) |
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