Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions.

Autor: Chen NC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Wang CH; Institute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan, ROC., Yoshimura M; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Yeh YQ; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Guan HH; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Chuankhayan P; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Lin CC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Lin PJ; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC.; Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 30043, Taiwan, ROC., Huang YC; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC., Wakatsuki S; Department of Structural Biology, Stanford University, Stanford, CA, 94305, USA.; SLAC National Accelerator Laboratory, Stanford Synchrotron Radiation Lightsource, Structural Molecular Biology, Menlo Park, CA, 94025, USA., Ho MC; Institute of Biological Chemistry, Academia Sinica, Taipei, 115, Taiwan, ROC. Joeho@gate.sinica.edu.tw., Chen CJ; Life Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, 30076, Taiwan, ROC. cjchen@nsrrc.org.tw.; Department of Physics, National Tsing Hua University, Hsinchu, 30043, Taiwan, ROC. cjchen@nsrrc.org.tw.; Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan, 701, Taiwan, ROC. cjchen@nsrrc.org.tw.; Department of Biological Science and Technology, National Yang Ming Chiao Tung University, Hsinchu, 30010, Taiwan, ROC. cjchen@nsrrc.org.tw.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2023 Feb 01; Vol. 14 (1), pp. 545. Date of Electronic Publication: 2023 Feb 01.
DOI: 10.1038/s41467-023-36235-3
Abstrakt: 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.
(© 2023. The Author(s).)
Databáze: MEDLINE
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