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

Tsimbalyuk, S.; Cross, E.M.; Hoad, Mikayla; Donnelly, Camilla M.; Roby, Justin A; Forwood, Jade K.

doi:10.3390/cells11081290

Cells

2022

DOI: 10.3390/cells11081290

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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

S. Tsimbalyuk¹,

E.M. Cross²,

Mikayla Hoad³

et al.

Abstract: The authors would like to make the following corrections to the published paper [...]

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The Disorderly Nature of Caliciviruses

Young,

McSweeney,

Edwards

et al. 2024

Viruses

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An intrinsically disordered protein (IDP) or region (IDR) lacks or has little protein structure but still maintains function. This lack of structure creates flexibility and fluidity, allowing multiple protein conformations and potentially transient interactions with more than one partner. Caliciviruses are positive-sense ssRNA viruses, containing a relatively small genome of 7.6–8.6 kb and have a broad host range. Many viral proteins are known to contain IDRs, which benefit smaller viral genomes by expanding the functional proteome through the multifunctional nature of the IDR. The percentage of intrinsically disordered residues within the total proteome for each calicivirus type species can range between 8 and 23%, and IDRs have been experimentally identified in NS1-2, VPg and RdRP proteins. The IDRs within a protein are not well conserved across the genera, and whether this correlates to different activities or increased tolerance to mutations, driving virus adaptation to new selection pressures, is unknown. The function of norovirus NS1-2 has not yet been fully elucidated but includes involvement in host cell tropism, the promotion of viral spread and the suppression of host interferon-λ responses. These functions and the presence of host cell-like linear motifs that interact with host cell caspases and VAPA/B are all found or affected by the disordered region of norovirus NS1-2. The IDRs of calicivirus VPg are involved in viral transcription and translation, RNA binding, nucleotidylylation and cell cycle arrest, and the N-terminal IDR within the human norovirus RdRP could potentially drive liquid–liquid phase separation. This review identifies and summarises the IDRs of proteins within the Caliciviridae family and their importance during viral replication and subsequent host interactions.

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The Disorderly Nature of Caliciviruses

Young,

McSweeney,

Edwards

et al. 2024

Viruses

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show abstract

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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

Abstract: The authors would like to make the following corrections to the published paper [...]

Cited by 1 publication

References 2 publications

The Disorderly Nature of Caliciviruses

The Disorderly Nature of Caliciviruses

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