ArticleThe Journal of biological chemistry2015
Vaccinia virus protein A49 is an unexpected member of the B-cell Lymphoma (Bcl)-2 protein family.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- Poxvirus A52 protein subverts autophagy flux by blocking autophagosome-lysosome fusion to promote viral replication.PLoS pathogens · 2026Article
- Recent advances in the inference of deep viral evolutionary history.Journal of virology · 2025Review
- Temporal expression classes and functions of vaccinia virus and mpox (monkeypox) virus genes.mBio · 2025Review
- The nuclear localization signal of monkeypox virus protein P2 orthologue is critical for inhibition of IRF3-mediated innate immunity.Emerging microbes & infections · 2024Article
- Viral-mediated activation and inhibition of programmed cell death.PLoS pathogens · 2022Review
- The actin nucleator Spir-1 is a virus restriction factor that promotes innate immune signalling.PLoS pathogens · 2022Article
- The crystal structure of vaccinia virus protein E2 and perspectives on the prediction of novel viral protein folds.The Journal of general virology · 2022Article
- Structural and molecular basis for Cardiovirus 2A protein as a viral gene expression switch.Nature communications · 2021Article
- Poxvirus Interactions with the Host Ubiquitin System.Pathogens (Basel, Switzerland) · 2021Review
- pUL21 is a viral phosphatase adaptor that promotes herpes simplex virus replication and spread.PLoS pathogens · 2021Article
- African Swine Fever Virus Ubiquitin-Conjugating Enzyme Is an Immunomodulator Targeting NF-κB Activation.Viruses · 2021Article
- Poxviral Strategies to Overcome Host Cell Apoptosis.Pathogens (Basel, Switzerland) · 2020Review
- Leaky scanning translation generates a second A49 protein that contributes to vaccinia virus virulence.The Journal of general virology · 2020Article
- The Bcl-2 Family: Ancient Origins, Conserved Structures, and Divergent Mechanisms.Biomolecules · 2020Review
- Vaccinia Virus Activation and Antagonism of Cytosolic DNA Sensing.Frontiers in immunology · 2020Review
- Unraveling virus relationships by structure-based phylogenetic classification.Virus evolution · 2020Review
- Molecular basis of cullin-3 (Cul3) ubiquitin ligase subversion by vaccinia virus protein A55.The Journal of biological chemistry · 2019Article
- NF-κB activation is a turn on for vaccinia virus phosphoprotein A49 to turn off NF-κB activation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Genetics of Life and Death: Virus-Host Interactions Underpinning Resistance to African Swine Fever, a Viral Hemorrhagic Disease.Frontiers in genetics · 2019Review
- Cullin-5 Adaptor SPSB1 Controls NF-κB Activation Downstream of Multiple Signaling Pathways.Frontiers in immunology · 2019Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Vaccinia virus (VACV) encodes several proteins that inhibit activation of the proinflammatory transcription factor nuclear factor κB (NF-κB). VACV protein A49 prevents translocation of NF-κB to the nucleus by sequestering cellular β-TrCP, a protein required for the degradation of the inhibitor of κB. A49 does not share overall sequence similarity with any protein of known structure or function. We solved the crystal structure of A49 from VACV Western Reserve to 1.8 Å resolution and showed, surprisingly, that A49 has the same three-dimensional fold as Bcl-2 family proteins despite lacking identifiable sequence similarity. Whereas Bcl-2 family members characteristically modulate cellular apoptosis, A49 lacks a surface groove suitable for binding BH3 peptides and does not bind proapoptotic Bcl-2 family proteins Bax or Bak. The N-terminal 17 residues of A49 do not adopt a single well ordered conformation, consistent with their proposed role in binding β-TrCP. Whereas pairs of A49 molecules interact symmetrically via a large hydrophobic surface in crystallo, A49 does not dimerize in solution or in cells, and we propose that this hydrophobic interaction surface may mediate binding to a yet undefined cellular partner. A49 represents the eleventh VACV Bcl-2 family protein and, despite these proteins sharing very low sequence identity, structure-based phylogenetic analysis shows that all poxvirus Bcl-2 proteins are structurally more similar to each other than they are to any cellular or herpesvirus Bcl-2 proteins. This is consistent with duplication and diversification of a single BCL2 family gene acquired by an ancestral poxvirus.
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