ArticleThe Journal of biological chemistry2016
The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Vaccinia virus F1L blocks the ribotoxic stress response to subvert ZAKα-dependent NLRP1 inflammasome activation.European journal of immunology · 2024Article
- Review
- Cross-species transmission and host range genes in poxviruses.Virologica Sinica · 2024Review
- Contribution of yeast models to virus research.Applied microbiology and biotechnology · 2021Review
- Poxviral Strategies to Overcome Host Cell Apoptosis.Pathogens (Basel, Switzerland) · 2020Review
- The Bcl-2 Family: Ancient Origins, Conserved Structures, and Divergent Mechanisms.Biomolecules · 2020Review
- Crystal Structure of African Swine Fever Virus A179L with the Autophagy Regulator Beclin.Viruses · 2019Article
- Vaccinia Virus Encodes a Novel Inhibitor of Apoptosis That Associates with the Apoptosome.Journal of virology · 2017Article
- Structural and Functional Insight into Canarypox Virus CNP058 Mediated Regulation of Apoptosis.Viruses · 2017Article
- The Bcl-2 Family in Host-Virus Interactions.Viruses · 2017Review
- Review
- Structural basis of apoptosis inhibition by the fowlpox virus protein FPV039.The Journal of biological chemistry · 2017Article
- Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins.PLoS pathogens · 2016Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Subversion of host cell apoptotic responses is a prominent feature of viral immune evasion strategies to prevent premature clearance of infected cells. Numerous poxviruses encode structural and functional homologs of the Bcl-2 family of proteins, and vaccinia virus harbors antiapoptotic F1L that potently inhibits the mitochondrial apoptotic checkpoint. Recently F1L has been assigned a caspase-9 inhibitory function attributed to an N-terminal α helical region of F1L spanning residues 1-15 (1) preceding the domain-swapped Bcl-2-like domains. Using a reconstituted caspase inhibition assay in yeast we found that unlike AcP35, a well characterized caspase-9 inhibitor from the insect virus Autographa californica multiple nucleopolyhedrovirus, F1L does not prevent caspase-9-mediated yeast cell death. Furthermore, we found that deletion of the F1L N-terminal region does not impede F1L antiapoptotic activity in the context of a viral infection. Solution analysis of the F1L N-terminal regions using small angle x-ray scattering indicates that the region of F1L spanning residues 1-50 located N-terminally from the Bcl-2 fold is an intrinsically unstructured region. We conclude that the N terminus of F1L is not involved in apoptosis inhibition and may act as a regulatory element in other signaling pathways in a manner reminiscent of other unstructured regulatory elements commonly found in mammalian prosurvival Bcl-2 members including Bcl-xL and Mcl-1.
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