ArticleJournal of virology2002
Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 77 citations in OpenAlex.
- CXCR4 chemokine receptor signaling induces apoptosis in acute myeloid leukemia cells via regulation of the Bcl-2 family members Bcl-XL, Noxa, and Bak.The Journal of biological chemistry · 2013Trial
- Molluscum Contagiosum Virus: Biology and Immune Response.Advances in experimental medicine and biology · 2024Review
- Review
- Review
- Poxviral Strategies to Overcome Host Cell Apoptosis.Pathogens (Basel, Switzerland) · 2020Review
- Review
- The molluscum contagiosum virus death effector domain containing protein MC160 RxDL motifs are not required for its known viral immune evasion functions.Virus genes · 2017Article
- Molecular architecture of the DED chains at the DISC: regulation of procaspase-8 activation by short DED proteins c-FLIP and procaspase-8 prodomain.Cell death and differentiation · 2016Article
- Structural insights of homotypic interaction domains in the ligand-receptor signal transduction of tumor necrosis factor (TNF).BMB reports · 2016Review
- Functional Comparison of Molluscum Contagiosum Virus vFLIP MC159 with Murine Cytomegalovirus M36/vICA and M45/vIRA Proteins.Journal of virology · 2015Article
- DED or alive: assembly and regulation of the death effector domain complexes.Cell death & disease · 2015Review
- Review
- Engagement of Fas on Macrophages Modulates Poly I:C induced cytokine production with specific enhancement of IP-10.PloS one · 2015Article
- Differential affinity of FLIP and procaspase 8 for FADD's DED binding surfaces regulates DISC assembly.Nature communications · 2014Article
- Inhibition of interferon gene activation by death-effector domain-containing proteins from the molluscum contagiosum virus.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The MC159 protein from the molluscum contagiosum poxvirus inhibits NF-κB activation by interacting with the IκB kinase complex.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- When autophagy meets viruses: a double-edged sword with functions in defense and offense.Seminars in immunopathology · 2010Review
- Going up in flames: necrotic cell injury and inflammatory diseases.Cellular and molecular life sciences : CMLS · 2010Review
- Viral cell death inhibitor MC159 enhances innate immunity against vaccinia virus infection.Journal of virology · 2010Article
- The molecular regulation of programmed necrotic cell injury.Trends in biochemical sciences · 2010Review
Corrections and comments
- Erratum issued
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Molluscum contagiosum virus (MCV), a member of the human poxvirus family, encodes the MC159 protein that inhibits Fas-, tumor necrosis factor (TNF)-, and TNF-related apoptosis-inducing ligant (TRAIL)-induced apoptosis. We used site-directed mutagenesis to change charged or hydrophobic amino acid residues to alanines to identify regions of MC159 that are critical for protection from apoptosis and for protein-protein interactions. Surprisingly, while MC159 is thought to block apoptosis by binding to Fas-associated death domain (FADD) or caspase-8, several mutants that lost apoptosis blocking activity still bound to both FADD and caspase-8. Mutations in the predicted hydrophobic patch 1 and alpha2 regions of both death effector domains (DEDs) within MC159 resulted in loss of the ability to bind to FADD or caspase-8 and to block apoptosis. Amino acid substitutions in the RXDL motif located in the alpha6 region of either DED resulted in loss of protection from apoptosis induced by Fas, TNF, and TRAIL and abolished the ability of MC159 to block death effector filament formation. Thus, charged or hydrophobic amino acids in three regions of the MC159 DEDs (hydrophobic patch 1, alpha2, and alpha6) are critical for the protein's ability to interact with cellular proteins and to block apoptosis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.