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Association·arcadia

Viruses use mimicry to modulate host immunity

Claim that viruses, especially large dsDNA viruses, use protein mimicry to alter or modulate the host immune response.

Confidence
90%
active

Evidence Quote

“Viruses use protein mimicry to modulate host immunity.”

Relationship

viral proteins modulates Host anti-parasite immune response

Arguments

Viral capsid proteinsubject
Host anti-parasite immune responseobject

Connections (10)

Reasoning connecting viral mimicry, immune modulation, and detection pipeline utilityInferenceChain
Petabase-scale sequence alignment increases viral discoveryAssociation
True structural mimicryFactor
Large dsDNA viruses are known to use protein mimicryAssociation
Evidence and reasoning on viral mimicry modulating immunity and detectionInferenceChain
Viral mimicry modulates host immunity via multiple structural mechanismsInferenceChain
Viral Bcl-2 homologs inhibit host apoptosisInferenceChain
Vaccinia virus complement evasion mechanismsInferenceChain
IL-10 and viral IL-10 homologs modulate immune responsesInferenceChain
Poxvirus mediated IFN-γ immune evasion mechanismInferenceChain

Evidence

“Reference: Alcami A. (2003), describing viral mimicry of immune signaling molecules.”

Alcami A. (2003). Viral mimicry of cytokines, chemokines and their receptors doi:10.1038/nri980 ↗

“Reference on molecular mimicry enabling viral immune evasion and potential autoimmunity.”

Maguire C et al. (2024). Molecular mimicry as a mechanism of viral immune evasion and autoimmunity doi:10.1038/s41467-024-53658-8 ↗

“Summarizes identification of capsid-like proteins in venomous and parasitic animals as reported by Borges et al.”

Borges et al. on capsid-like proteins in venomous and parasitic animals

“Evidence synthesizing that molecular mimicry by viruses enables immune evasion and triggers autoimmunity, from Maguire et al. (2024).”

Maguire C, Wang C et al. (2024). Molecular mimicry as a mechanism of viral immune evasion and autoimmunity.

“Reference describing language model-based prediction of atomic-level protein structures at evolutionary scale.”

(2023). Evolutionary-scale prediction of atomic-level protein structure with a language model doi:10.1126/science.ade2574 ↗

“Reference describing the solution structure of EBV BHRF1 protein, which is homologous to human Bcl-2.”

Huang Q et al. (2003). Solution Structure of the BHRF1 Protein From Epstein-Barr Virus, a Homolog of Human Bcl-2 doi:10.1016/j.jmb.2003.08.007 ↗

“Reference detailing that EBV encodes a Bcl-2 homolog that inhibits apoptosis by associating with Bax and Bak.”

Marshall WL et al. (1999). Epstein-Barr Virus Encodes a Novel Homolog of the bcl-2 Oncogene That Inhibits Apoptosis and Associates with Bax and Bak doi:10.1128/jvi.73.6.5181-5185.1999 ↗

“Reference showing that structural homology screens identify poxvirus protein families derived from host that modulate inflammasome activity.”

Boys IN et al. (2023). Structural homology screens reveal host-derived poxvirus protein families impacting inflammasome activity doi:10.1016/j.celrep.2023.112878 ↗

“Reference describing vaccinia virus complement control protein's role in preventing complement-enhanced neutralization and contributing to virulence.”

Isaacs SN et al. (1992). Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence doi:10.1073/pnas.89.2.628 ↗

“Reference describing vaccinia, cowpox and camelpox viruses encoding soluble gamma interferon receptors with broad species specificity.”

Alcamí A & Smith GL (1995). Vaccinia, cowpox, and camelpox viruses encode soluble gamma interferon receptors with novel broad species specificity doi:10.1128/jvi.69.8.4633-4639.1995 ↗

“Reference reporting overexpression of vaccinia virus A38L integral membrane protein promotes Ca2+ influx into infected cells.”

Sanderson CM et al. (1996). Overexpression of the vaccinia virus A38L integral membrane protein promotes Ca2+ influx into infected cells doi:10.1128/jvi.70.2.905-914.1996 ↗

“Reference identifying the vaccinia virus A38L gene product as a 33-kDa integral membrane glycoprotein.”

Parkinson JE et al. (1995). The Vaccinia Virus A38L Gene Product Is a 33-kDa Integral Membrane Glycoprotein doi:10.1006/viro.1995.9942 ↗

“Reference describing the crystal structure of Epstein-Barr virus protein BCRF1, homologous to cellular interleukin-10.”

Zdanov A et al. (1997). Crystal structure of epstein-barr virus protein BCRF1, a homolog of cellular interleukin-10 doi:10.1006/jmbi.1997.0990 ↗

“Reference discussing proteins with the same structure but different functions.”

Yoon SI et al. (2005). Same Structure, Different Function doi:10.1016/j.str.2005.01.016 ↗

“Reference reporting that human poxvirus-encoded proteins bind IL-18 and inhibit interferon gamma induction.”

IL-18 binding and inhibition of interferon γ induction by human poxvirus-encoded proteins doi:10.1073/pnas.96.20.11537 ↗

“Reference describing a novel inhibitor of apoptosis encoded by vaccinia virus and conserved in eukaryotes.”

Gubser C et al.. A New Inhibitor of Apoptosis from Vaccinia Virus and Eukaryotes doi:10.1371/journal.ppat.0030017 ↗

“Reference reporting that a human poxvirus chemokine homolog exhibits broad spectrum chemokine antagonistic activity.”

Damon I et al.. Broad spectrum chemokine antagonistic activity of a human poxvirus chemokine homolog doi:10.1073/pnas.95.11.6403 ↗

“Reference exploring viral protein structural mimicry guided by host interactions and implications for human disease.”

Lasso G et al.. A Sweep of Earth’s Virome Reveals Host-Guided Viral Protein Structural Mimicry and Points to Determinants of Human Disease doi:10.1016/j.cels.2020.09.006 ↗

“Reference describing how EBV BGLF4 kinase suppresses IRF3 signaling pathway, interfering with interferon response.”

Wang J-T et al.. Epstein-Barr Virus BGLF4 Kinase Suppresses the Interferon Regulatory Factor 3 Signaling Pathway doi:10.1128/jvi.01099-08 ↗

“Evidence line providing support for using the cited reference about Chlamydomonas flagellum as a model for human ciliary disease.”

The Chlamydomonas Flagellum as a Model for Human Ciliary Disease

“Evidence line supporting restoration of motility in Chlamydomonas mutants modeling spermatogenic failure as described in the cited reference.”

Rescuing Chlamydomonas motility in mutants modeling spermatogenic failure

“Evidence line describing phenotypes of a Chlamydomonas insertional mutant disrupting flagellar central pair microtubule-associated structures, supported by the cited reference.”

Characterization of a Chlamydomonas Insertional Mutant that Disrupts Flagellar Central Pair Microtubule-associated Structures

“Evidence line showing that actin cytoskeleton functions are conserved in absence of canonical actin-binding proteins, supported by the cited reference.”

Paredez AR et al. (2011) An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins

“Evidence supporting functional distinctions and conserved roles of actin gene family members and isoforms, as referenced by (2010) The actin gene family: Function follows isoform.”

(2010) The actin gene family: Function follows isoform