2021
DOI: 10.1002/1873-3468.14099
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K160 in the RNA‐binding domain of the orf virus virulence factor OV20.0 is critical for its functions in counteracting host antiviral defense

Abstract: The OV20.0 virulence factor of orf virus antagonizes host antiviral responses. One mechanism through which it functions is by inhibiting activation of the dsRNA-activated protein kinase R (PKR) by sequestering dsRNA and by physically interacting with PKR. Sequence alignment indicated that several key residues critical for dsRNA binding were conserved in OV20.0, and their contribution to OV20.O function was investigated in this study. We found that residues F141, K160, and R164 were responsible for the dsRNA-bi… Show more

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Cited by 2 publications
(8 citation statements)
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References 57 publications
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“…ΔC, which lacks the C‐terminal RBD, served as a negative control. Of note, K160A is an OV20.0 mutant deficient in binding with dsRNA and other OV20.0‐interacting proteins [20], including DGCR8 (Fig. S3).…”
Section: Resultsmentioning
confidence: 99%
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“…ΔC, which lacks the C‐terminal RBD, served as a negative control. Of note, K160A is an OV20.0 mutant deficient in binding with dsRNA and other OV20.0‐interacting proteins [20], including DGCR8 (Fig. S3).…”
Section: Resultsmentioning
confidence: 99%
“…1). Since DGCR8 is not required for shRNA production, this may partially explain why the failure of OV20.0 to suppress RNA interference via shRNA in mammalian cells [20] is likely due to the shRNA system bypassing the step of pri-miRNA processing.…”
Section: Discussionmentioning
confidence: 99%
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“…PACT can be targeted as a PKR evasion strategy. In addition to binding to dsRNA and PKR itself ( Liao et al, 2021 ), the Orf virus (ORFV)-encoded protein OV20.0 was shown to interact with PACT, thereby blocking PACT-mediated PKR activation ( Tseng et al, 2015 ).…”
Section: Mechanisms Of Pkr Inhibition By Virusesmentioning
confidence: 99%