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Errors in the deposited SFTSV L protein structure

Nature Microbiology volume 6, pages 549–550 (2021)Cite this article

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Matters Arising to this article was published on 29 April 2021

The Original Article was published on 27 April 2020

arising from P. Wang et al. Nature Microbiology https://doi.org/10.1038/s41564-020-0712-2 (2020)

We detected major errors in the cryogenic electron microscopy (cryo-EM) structure of the L protein (polymerase) of the severe fever with thrombocytopenia syndrome virus (SFTSV), published in April 2020 in Nature Microbiology1.

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Fig. 1: Comparison of the original model (6L42) with the rebuilt model (7ALP).
Fig. 2: Region 1422–1697.

References

  1. Wang, P. et al. Structure of severe fever with thrombocytopenia syndrome virus L protein elucidates the mechanisms of viral transcription initiation. Nat. Microbiol. 5, 864–871 (2020).

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  2. Vogel, D. et al. Structural and functional characterization of the severe fever with thrombocytopenia syndrome virus L protein. Nucleic Acids Res. 48, 5749–5765 (2020).

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  3. Wang, W. et al. The cap-snatching SFTSV endonuclease domain is an antiviral target. Cell Rep. 30, 153–163 (2020).

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  4. Afonine, P. V. et al. New tools for the analysis and validation of cryo-EM maps and atomic models. Acta Crystallogr. D. Struct. Biol. 74, 814–840 (2018).

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Author information

Authors and Affiliations

  1. European Molecular Biology Laboratory, Grenoble, France

    Stephen Cusack

  2. Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany

    Maria Rosenthal

Authors
  1. Stephen Cusack
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  2. Maria Rosenthal
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Contributions

S.C. and M.R. jointly rebuilt the model and prepared the manuscript.

Corresponding author

Correspondence to Stephen Cusack.

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The authors declare no competing interests.

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Cusack, S., Rosenthal, M. Errors in the deposited SFTSV L protein structure. Nat Microbiol 6, 549–550 (2021). https://doi.org/10.1038/s41564-021-00901-3

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  • DOI: https://doi.org/10.1038/s41564-021-00901-3

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