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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Proteins targeted to the nucleus carry short stretches of amino acid sequences called the nuclear localization signal or NLS. Classical nuclear localization signals are of two types: monopartite and bipartite NLS. Monopartite classical NLS (cNLS) consists of a single cluster of 4-8 amino acids. Bipartite cNLS consists of two clusters of  2-3 amino acids and a 9-12 residue long proline-rich linker bridging the two clusters. Signal clusters are rich in positively charged amino acids such as...
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Updated: Sep 9, 2025

Dissecting Innate Immune Signaling in Viral Evasion of Cytokine Production
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Měnglà Virus VP40 Localizes to the Nucleus and Impedes the RIG-I Signaling Pathway.

Joyce Sweeney Gibbons1, Naveen Thakur2, Emma Komers2

  • 1Center for Microbial Pathogenesis, Institute for Biomedical Sciences, Georgia State University, Atlanta, GA 30303, USA.

Viruses
|August 28, 2025
PubMed
Summary

Měnglà virus VP40 protein uniquely inhibits innate immune responses by interfering with interferon signaling pathways. This filovirus protein shows distinct nuclear localization and import mechanisms compared to Ebola and Marburg viruses.

Keywords:
Ebola virusMarburg virusMěnglà virusfilovirusimportininterferoninterferon regulatory factor 3 (IRF3)late-domain motifnuclear localization signal

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Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Měnglà virus (MLAV) is a filovirus with potential to affect human health.
  • MLAV VP35 and VP40 proteins can antagonize human innate immune defenses.
  • The specific mechanisms of MLAV VP40 immune evasion are not fully understood.

Purpose of the Study:

  • To investigate the immune evasion mechanisms of MLAV VP40.
  • To compare the functions of MLAV VP40 with those of Ebola virus (EBOV) and Marburg virus (MARV) VP40.

Main Methods:

  • Assessed MLAV VP40's effect on Sendai virus (SeV)-induced IFNβ promoter activation.
  • Compared MLAV VP40's inhibition of IFNβ and NF-κB signaling with EBOV and MARV VP40.
  • Investigated MLAV VP40's interaction with RIG-I, IRF3, TBK1, IKKε, and its subcellular localization.
  • Examined MLAV VP40's interaction with importin alpha-1 (IMPα1).

Main Results:

  • MLAV VP40 inhibited SeV-induced IFNβ promoter activation independently of its late-domain motif.
  • MLAV VP40 showed less inhibition of TNFα-induced NF-κB activation compared to IFNβ.
  • MLAV VP40 impaired IFNβ promoter activation by RIG-I, TBK1, and IKKε, but not constitutively active IRF3.
  • MLAV VP40 induced IRF3 phosphorylation and exhibited significant nuclear localization, interacting with IMPα1.
  • EBOV and MARV VP40 showed less nuclear localization and did not accumulate in nuclear foci.

Conclusions:

  • MLAV VP40 possesses distinct mechanisms for antagonizing innate immunity compared to EBOV and MARV VP40.
  • MLAV VP40's nuclear localization and interaction with IMPα1 are key distinguishing features.
  • These findings highlight novel aspects of MLAV VP40's immune evasion strategy.