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-Structure paper
| タイトル | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions. |
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| ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 545, Year 2023 |
| 掲載日 | 2023年2月1日 |
 著者 | Nai-Chi Chen / Chun-Hsiung Wang / Masato Yoshimura / Yi-Qi Yeh / Hong-Hsiang Guan / Phimonphan Chuankhayan / Chien-Chih Lin / Pei-Ju Lin / Yen-Chieh Huang / Soichi Wakatsuki / Meng-Chiao Ho / Chun-Jung Chen /   |
| PubMed 要旨 | Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM ...Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM structures of T = 4 and T = 3 capsids of virus-like particles (VLPs) of Lake Sinai virus (LSV) 2 and delta-N48 LSV1, belonging to tetraviruses, at resolutions of 2.3-2.6 Å in various pH environments. Structural analysis shows that the LSV2 capsid protein (CP) structural features, particularly the protruding domain and C-arm, differ from those of other tetraviruses. The anchor loop on the central β-barrel domain interacts with the neighboring subunit to stabilize homo-trimeric capsomeres during assembly. Delta-N48 LSV1 CP interacts with ssRNA via the rigid helix α1', α1'-α1 loop, β-barrel domain, and C-arm. Cryo-EM reconstructions, combined with X-ray crystallographic and small-angle scattering analyses, indicate that pH affects capsid conformations by regulating reversible dynamic particle motions and sizes of LSV2 VLPs. C-arms exist in all LSV2 and delta-N48 LSV1 VLPs across varied pH conditions, indicating that autoproteolysis cleavage is not required for LSV maturation. The observed linear domino-scaffold structures of various lengths, made up of trapezoid-shape capsomeres, provide a basis for icosahedral T = 4 and T = 3 architecture assemblies. These findings advance understanding of honeybee-infecting viruses that can cause Colony Collapse Disorder. |
 リンク | Nat Commun / PubMed:36726015 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.32 - 4.8 Å |
| 構造データ | EMDB-33368, PDB-7xpa: EMDB-33369, PDB-7xpb: EMDB-33370, PDB-7xpd: EMDB-33371, PDB-7xpe: EMDB-33372, PDB-7xpf: EMDB-33373, PDB-7xpg:  EMDB-33374: Focused refinement cryo-EM map of the A/B/C subunits of the T=4 lake sinai virus 2 virus-like particle at pH 7.5  EMDB-33375: Focus refinement cryo-EM map of the D/D/D subunits of the T=4 lake sinai virus 2 virus-like particle  EMDB-33376: Focused refinement cryo-EM map of the A/B/C subunits of the T=3 lake sinai virus 2 virus-like particle at pH 7.5  EMDB-33377: Focused refinement cryo-EM map of the A/B/C subunits of the T=4 lake sinai virus 2 virus-like particle at pH 6.5  EMDB-33378: Focused refinement cryo-EM map of the D/D/D subunits of the T=4 lake sinai virus 2 virus-like particle at pH 6.5  EMDB-33379: Focused refinement cryo-EM map of the A/B/C subunits of the T=3 lake sinai virus 2 virus-like particle at pH 6.5  EMDB-33380: Focused refinement cryo-EM map of the A/B/C subunits of the T=4 lake sinai virus 2 virus-like particle at pH 8.5  EMDB-33381: Focused refinement cryo-EM map of the D/D/D subunits of the T=4 lake sinai virus 2 virus-like particle at pH 8.5  EMDB-33382: Focused refinement cryo-EM map of the A/B/C subunits of the T=3 lake sinai virus 2 virus-like particle at pH 8.5  EMDB-33383: Focused refinement cryo-EM map of the A/B/C subunits of the T=3 lake sinai virus 1 (delta N-terminal 48 residues) virus-like particle at pH 6.5  EMDB-33384: Cryo-EM map of the T=4 lake sinai virus 1 (delta N-terminal 48 residues) virus-like particle at pH 6.5 |
| 由来 |
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 キーワード | VIRUS LIKE PARTICLE |
lake sinai virus 2 (ウイルス)
escherichia coli (大腸菌)