Nucleic Acids Research, Volume 48, Issue 10, 04 June 2020, Pages 5749–5765, https://doi.org/10.1093/nar/gkaa253
In the biochemical characterization of SFTSV L protein, cRNA sequences were used instead of vRNA sequences. This does not undermine any of the scientific conclusions made in the paper as bunyaviruses use both cRNA and vRNA as templates for genome replication. Within the terminal 10 nucleotides, there is only one nucleotide different between the cRNA and the vRNA in the SFTSV strain used (Figure 1).
Figure 1.
Comparison between vRNA and cRNA in SFTSV. The terminal 20 nucleotides of the vRNA (negative/genomic sense) and cRNA (positive/antigenomic sense) of SFTSV strain AH12 are compared. Complementarity between 3′ and 5′ RNA termini is highlighted in green.
The following corrections of the publication ‘Structural and functional characterization of the Severe fever with thrombocytopenia syndrome virus L protein’ are necessary.
We also refer readers to our online comment (https://academic.oup.com/nar/article/48/10/5749/5822961#usercomments) which describes the problem of viral sequence nomenclature and the need for standardization in the GenBank database.
In the Results:
The SFTSV L protein RdRp was only active when both the 3′ template vRNA and the 5′ vRNA were present in the reaction (Figure 3B).
should be
The SFTSV L protein RdRp was only active when both the 3′ template RNA and the 5′ RNA were present in the reaction (Figure 3B).
Also in the Results:
We conclude that SFTSV initiates genome replication on a vRNA template either terminally and without applying a prime-and-realign mechanism similar to influenza virus cRNA synthesis (22) or by priming at position + 3 and subsequent realignment to the terminal position + 1 (Figure 4D).
should be
We conclude that SFTSV initiates genome replication on a cRNA template either terminally and without applying a prime-and-realign mechanism similar to influenza virus cRNA synthesis (22) or by priming at position + 3 and subsequent realignment to the terminal position + 1 (Figure 4D).
In the Conclusions:
Furthermore, we show that that SFTSV L likely initiates genome replication on vRNA de novo without applying a prime-and-realign mechanism and that cap-dependent transcription requires an unknown switch.
should be
Furthermore, we show that that SFTSV L likely initiates genome replication on cRNA de novo without applying a prime-and-realign mechanism and that cap-dependent transcription requires an unknown switch.
In the Supplement:
Supplementary Figure S6. Binding of the conserved vRNA promoter ends to the SFTSV L protein.
should be
Supplementary Figure S6. Binding of the conserved RNA promoter ends to the SFTSV L protein.
Also in the Supplement:
Supplementary Figure S12. Additional results from biochemical in vitro assays.
(A) The potential influence of a 5′ single nucleotide C overhang on the polymerase activity of SFTSV L (D112A) was tested. The protein was incubated with the 5′ vRNA either with or without an additional C and/or 3′ terminal 20 nt of the M segment (5′ M: HOACACAGAGACGGCCAACAAU-OH, 5′ M + C: HO-CACACAGAGACGGCCAACAAU-OH 3′ M: HO-UGUGUUUCUGGCCGGUUGUG-OH, Supplementary Table S1) under standard polymerase assay conditions (see Materials and Methods).
should be
Supplementary Figure S12. Additional results from biochemical in vitro assays.
(A) The potential influence of a 5′ single nucleotide C overhang on the polymerase activity of SFTSV L (D112A) was tested. The protein was incubated with the 5′ cRNA either with or without an additional C and/or 3′ terminal 20 nt of the M segment (5′ M: HOACACAGAGACGGCCAACAAU-OH, 5′ M + C: HO-CACACAGAGACGGCCAACAAU-OH 3′ M: HO-UGUGUUUCUGGCCGGUUGUG-OH, Supplementary Table S1) under standard polymerase assay conditions (see Materials and Methods).
These details have been corrected only in this correction notice to preserve the published version of record.