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. 2025 Dec 16;15:1762181. doi: 10.3389/fcimb.2025.1762181

Correction: Distinct ZIKV strain signatures and type I IFN modulation reveal a protective role of brain endothelial interferon signaling in vitro and in vivo

Luan Rocha Lima 1, Yasmin Mucunã Mustafá 1, Paula Luize Camargos Fonseca 2, Sharton Vinícius Antunes Coelho 1, Pierina Lorencini Parisi 3, Camila Lopes Simeoni 3, Lana Monteiro Meuren 1, Bruno Braz Bezerra 1, Nathane Cunha Mebus-Antunes 4, Flavio Matassoli 1,5, Jose Luiz Proença-Modena 3, Renato Santana Aguiar 2,6, Luciana Barros de Arruda 1,*
PMCID: PMC12752108  PMID: 41477001

There was a mistake in Figure 5 as published. An arrow indicating a modification in the 5’UTR was missing in Figures 5A, B, and one of the colors did not match the legend in Figure 5E. The corrected Figure 5 appears below.

Figure 5.

(A) and (B) Illustrate stem-loop structures in the 5’ UTRs of two ZIKV strains, PE243 and MR766, with numbered sequences. (C) Shows NS5 protein domains MTase and RdRp, with mutation sites. (D) Depicts NS5 protein structure with labeled MTase and RdRp regions and key residues. (E) Shows ZIKV capsid protein structure with helices labeled. (F) Displays N-terminal and alpha-helix regions of the ZIKV capsid protein with mutation sites.

Comparison of genomic and amino acid sequences by the 5’UTR, NS5 and capsid protein from ZIKVMR766 (NC_012532.1) and ZIKVPE243 (GenBank KX197192.1). (A, B) Sequence and predicted secondary structure of stem-loop A in the 5′UTRs from ZIKVPE243(A) and ZIKVMR766(B). The black arrows indicate sequence variations in the 5′-UTR. (C) Schematic representation of ZIKV NS5 from ZIKVMR766 indicating the amino acid substitutions in the NS5 from ZIKVPE243. MTase and RdRp domains are colored purple and gray, respectively. (D) Ribbon representation showing the MTase (light pink) and RdRp (gray) domains of ZIKVMR766 NS5. The locations of residues that differed in NS5 from ZIKVPE243 in the context of ZIKVMR766 NS5 structure (PDB, 5U0B) are shown in orange sticks. The residues Y25, R327, D734 and H855 are highlighted in blue sticks, and the K252 residue (green stick) is labeled in orange. (E) Ribbon representation showing the structure of the ZIKV capsid protein (PDB, 6C44), with the α-helix pairs indicated: α1/α1’ (purple), α2/α2’ (red), α3/α3’ (brown), and α4/α4’ (blue). (F) Schematic representation of the capsid protein from ZIKVPE243 indicating the amino acid substitutions from ZIKVMR766. The α-helices are colored according to protein structure in (E).

The original version of this article has been updated.

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