ArticleThe Journal of biological chemistry2019
Myxoma virus M013 protein antagonizes NF-κB and inflammasome pathways via distinct structural motifs.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- Mammalian innate antiviral defenses: beyond interferon.Journal of virology · 2025Review
- The Role of Myxoma Virus Immune Modulators and Host Range Factors in Pathogenesis and Species Leaping.Viruses · 2025Review
- Modulation of retinal inflammation delays degeneration in a mouse model of geographic atrophy.Scientific reports · 2025Article
- The poxvirus F17 protein counteracts mitochondrially orchestrated antiviral responses.Nature communications · 2023Article
- Structural homology screens reveal host-derived poxvirus protein families impacting inflammasome activity.Cell reports · 2023Article
- Structural homology screens reveal poxvirus-encoded proteins impacting inflammasome-mediated defenses.bioRxiv : the preprint server for biology · 2023Article
- Poxviruses and the immune system: Implications for monkeypox virus.International immunopharmacology · 2022Review
- Battle Royale: Innate Recognition of Poxviruses and Viral Immune Evasion.Biomedicines · 2021Review
- Chikungunya Virus nsP2 Impairs MDA5/RIG-I-Mediated Induction of NF-κB Promoter Activation: A Potential Target for Virus-Specific Therapeutics.Journal of microbiology and biotechnology · 2020Article
- AAV Mediated Delivery of Myxoma Virus M013 Gene Protects the Retina against Autoimmune Uveitis.Journal of clinical medicine · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Among the repertoire of immunoregulatory proteins encoded by myxoma virus, M013 is a viral homologue of the viral pyrin domain-only protein (vPOP) family. In myeloid cells, M013 protein has been shown to inhibit both the inflammasome and NF-κB signaling pathways by direct binding to ASC1 and NF-κB1, respectively. In this study, a three-dimensional homology model of the M013 pyrin domain (PYD) was built based on similarities to known PYD structures. A distinctive feature of the deduced surface electrostatic map of the M013 PYD is the presence of a negatively region consisting of numerous aspartate and glutamate residues in close proximity. Single-site mutations of aspartate and glutamate residues reveal their role in interactions with ASC-1. The biological significance of charge complementarity in the M013-ASC-1 interaction was further confirmed by functional assays of caspase-1 activation and subsequent secretion of cytokines. M013 also has a unique 33-residue C-terminal tail that follows the N-terminal PYD, and it is enriched in positively charged residues. Deletion of the tail of M013 significantly inhibited the interactions between M013 and NF-κB1, thus compromising the ability of the viral protein to suppress the secretion of pro-inflammatory cytokines. These results demonstrate that vPOP M013 exploits distinct structural motifs to regulate both the inflammasome and NF-κB pathways.
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