Journal article
Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly
Structure (London), v 32(8), pp 1068-1078
08 Aug 2024
PMID: 38749445
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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.
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•The trimeric THOV NP crystal structure was determined•RNA-binding groove of THOV NP was identified•THOV NP tail loop mutations interfere with oligomerization and viral replication•A cryo-ET reconstruction of THOV RNP revealed a left-handed helical architecture
Dick et al. determined structures of the trimeric orthomyxovirus Thogoto virus nucleoprotein and the native ribonucleoprotein complex. They identified and functionally characterized the RNA-binding groove and the oligomerization mode. Their study elucidates promising sites for the development of antivirals drugs, which interfere with RNA binding or oligomerization.
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Details
- Title
- Structural characterization of Thogoto Virus nucleoprotein provides insights into viral RNA encapsidation and RNP assembly
- Creators
- Alexej Dick - Drexel University, Biochemistry and Molecular BiologyVasilii Mikirtumov - Max Delbrück CenterJonas Fuchs - University of FreiburgFerdinand Krupp - Max Delbrück CenterDaniel Olal - Max Delbrück CenterElias Bendl - University of FreiburgThiemo Sprink - Max Delbrück CenterChristoph Diebolder - Charité - Universitätsmedizin BerlinMikhail Kudryashev - Max Delbrück CenterGeorg Kochs - University of FreiburgYvette Roske - Max Delbrück CenterOliver Daumke - Max Delbrück Center
- Publication Details
- Structure (London), v 32(8), pp 1068-1078
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:001292205800001
- Scopus ID
- 2-s2.0-85194587600
- Other Identifier
- 991021877915704721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics
- Cell Biology