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Structure paper

TitleStructural and functional characterization of the severe fever with thrombocytopenia syndrome virus L protein.
Journal, issue, pagesNucleic Acids Res, Vol. 48, Issue 10, Page 5749-5765, Year 2020
Publish dateJun 4, 2020
AuthorsDominik Vogel / Sigurdur Rafn Thorkelsson / Emmanuelle R J Quemin / Kristina Meier / Tomas Kouba / Nadja Gogrefe / Carola Busch / Sophia Reindl / Stephan Günther / Stephen Cusack / Kay Grünewald / Maria Rosenthal /
PubMed AbstractThe Bunyavirales order contains several emerging viruses with high epidemic potential, including Severe fever with thrombocytopenia syndrome virus (SFTSV). The lack of medical countermeasures, such ...The Bunyavirales order contains several emerging viruses with high epidemic potential, including Severe fever with thrombocytopenia syndrome virus (SFTSV). The lack of medical countermeasures, such as vaccines and antivirals, is a limiting factor for the containment of any virus outbreak. To develop such antivirals a profound understanding of the viral replication process is essential. The L protein of bunyaviruses is a multi-functional and multi-domain protein performing both virus transcription and genome replication and, therefore, is an ideal drug target. We established expression and purification procedures for the full-length L protein of SFTSV. By combining single-particle electron cryo-microscopy and X-ray crystallography, we obtained 3D models covering ∼70% of the SFTSV L protein in the apo-conformation including the polymerase core region, the endonuclease and the cap-binding domain. We compared this first L structure of the Phenuiviridae family to the structures of La Crosse peribunyavirus L protein and influenza orthomyxovirus polymerase. Together with a comprehensive biochemical characterization of the distinct functions of SFTSV L protein, this work provides a solid framework for future structural and functional studies of L protein-RNA interactions and the development of antiviral strategies against this group of emerging human pathogens.
External linksNucleic Acids Res / PubMed:32313945 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.35 - 3.78 Å
Structure data

10706

6y6k

EMDB-10706, PDB-6y6k:
Cryo-EM structure of a Phenuiviridae L protein
Method: EM (single particle) / Resolution: 3.78 Å

PDB-6xya:
Cap-binding domain of SFTSV L protein
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

Chemicals

ChemComp-MGP:
7-METHYL-GUANOSINE-5'-TRIPHOSPHATE

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-MG:
Unknown entry

Source
  • sfts virus ah12
KeywordsVIRAL PROTEIN / bunyavirus / cap binding / cap-snatching / viral polymerase / Phenuiviridae / L protein

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