Correction: Tsimbalyuk et al. The Intrinsically Disordered W Protein Is Multifunctional during Henipavirus Infection, Disrupting Host Signalling Pathways and Nuclear Import (Cells 2020, 9, 1913)

Sofiya Tsimbalyuk, Emily M. Cross, Mikayla Hoad, Camilla M. Donnelly, A. Roby Justin, Jade K. Forwood

Research output: Contribution to journalComment/debatepeer-review

Abstract

Text Correction: The authors would like to make the following corrections to the published paper [1]: There are some mistakes in the order of references and their citations in the original article due to bibliography software errors [1]. In the original publication, Shaw, M.L. et al., 2004 was reference 20 in the reference list, and now that we have updated the reference list as below (Reference List Correction), it has become reference 39. Consequently, we have also updated the citation number in Section 5.3. WProtein Binds Host STAT to Create HighMolecular Weight Complexes that Inhibit Type I IFN Signalling, page 10, which should now read: The W protein has been found to be the dominant STAT-1 inhibitor compared to V/P/C counterparts [39,87]. Unlike V, C, and P proteins that are mostly cytoplasmic, theW protein of NiV co-localizes to the nucleus with STAT-1 in its unphosphorylated form [39]. This indicates that W either binds STAT-1 in the nucleus, preventing its nuclear export and recycling in the JAK-STAT pathway, or transports latent (and unphosphorylated) STAT-1 directly to the nucleus where W then sequesters it as a high molecular weight non-functional complex (Figure 4) [39].

Original languageEnglish
Article number1290
JournalCells
Volume11
Issue number8
DOIs
Publication statusPublished - 01 Apr 2022

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