Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly

被引:4
作者
Dick, Alexej [1 ,2 ,6 ]
Mikirtumov, Vasilii [1 ,2 ]
Fuchs, Jonas [3 ]
Krupp, Ferdinand [1 ]
Olal, Daniel [1 ]
Bendl, Elias [3 ]
Sprink, Thiemo [1 ,4 ]
Diebolder, Christoph [4 ]
Kudryashev, Mikhail [1 ,5 ]
Kochs, Georg [3 ]
Roske, Yvette [1 ]
Daumke, Oliver [1 ,2 ]
机构
[1] Max Delbruck Ctr Mol Med Helmholtz Assoc, Struct Biol, Robert-Rossle-Straf3e 10, D-13125 Berlin, Germany
[2] Free Univ Berlin, Inst Chem & Biochem, D-14195 Berlin, Germany
[3] Univ Freiburg, Inst Virol, Fac Med, Hermann-Herder-Str 11, D-79104 Freiburg, Germany
[4] Core facil Cryo Electron Microscopy Charite, Berlin, Germany
[5] Charite Univ Med Berlin, Inst Med Phys & Biophys, Berlin, Germany
[6] Drexel Univ, Dept Biochem & Mol Biol, Coll Med, 245 North 15th St,New Coll Bldg, Philadelphia, PA 19102 USA
关键词
HUMAN MXA PROTEIN; CRYO-EM; INFLUENZA; BINDING; TOMOGRAPHY; OLIGOMERIZATION; MECHANISM; TOOLS; MODEL; TILT;
D O I
10.1016/j.str.2024.04.016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Orthomyxoviruses, such as influenza and thogotoviruses, are important human and animal pathogens. Their segmented viral RNA genomes are wrapped by viral nucleoproteins (NPs) into helical ribonucleoprotein complexes (RNPs). NP structures of several influenza viruses have been reported. However, there are still contradictory models of how orthomyxovirus RNPs are assembled. Here, we characterize the crystal structure of Thogoto virus (THOV) NP and found striking similarities to structures of influenza viral NPs, including a two-lobed domain architecture, a positively charged RNA-binding cleft, and a tail loop important for trimerization and viral transcription. A low-resolution cryo-electron tomography reconstruction of THOV RNPs elucidates a left-handed double helical assembly. By providing a model for RNP assembly of THOV, our study suggests conserved NP assembly and RNA encapsidation modes for thogoto- and influenza viruses.
引用
收藏
页码:1068 / 1078.e5
页数:17
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