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Human MAVS Protein expressed in HEK-293 Cells - ABIN2725562
He, Zhu, Wen, Yuan, Hu, Chen, An, Dong, Lin, Yu, Wu, Yang, Cai, Li, Li: Dengue Virus Subverts Host Innate Immunity by Targeting Adaptor Protein MAVS. in Journal of virology 2016
The mitochondrial antiviral signaling adaptor protein (MAVS) oligomers and high MW aggregates coexist upon constitutively active retinoic acid-inducible gene I (RIG-I) ectopic expression and virus infection. Anchoring of MAVS to intracellular membranes is essential for an appropriate polymerization process allowing functional high MW aggregates to occur.
MAVS isoforms are truncated, which prevents its spontaneous aggregation in antiviral innate immune signalling
these results demonstrated that HAUS8 may function as a positive regulator of RLRVISA dependent antiviral signaling by targeting the VISA complex, providing a novel regulatory mechanism of antiviral responses
results suggest that ASC, as a negative regulator of the MAVS-mediated innate immunity, may play an important role in host protection upon virus infection
Using MAVS as a platform, NLRP11 degrades TRAF6 to attenuate the production of type I IFNs as well as virus-induced apoptosis. Our findings reveal the regulatory role of NLRP11 in antiviral immunity by disrupting MAVS signalosome.
Low MAVS expression is associated with RNA virus infections.
MCCC1 plays an essential role in virus-triggered, MAVS-mediated activation of NF-kappaB signaling.
The down regulation of TRIF, TLR3, and mitochondrial antiviral signaling protein (MAVS) expressions in chronic hepatitis C correlates with the disease severity and the outcome of hepatitis C virus infection
Taken together, these findings reveal an essential role of CypA in boosting RIG-I-mediated antiviral immune responses by controlling the ubiquitination of RIG-I and MAVS.
Data show that human cytomegalovirus (HCMV; human betaherpesvirus 5) glycoprotein US9 inhibits the IFN-beta response by targeting the mitochondrial antiviral-signaling protein (MAVS) and stimulator of interferon genes (STING)-mediated signaling pathways.
our results demonstrate that miR-22 negatively regulates poly(I:C)-induced production of type I interferon and inflammatory cytokines via targeting MAVS.
this analysis did not indicate the association of the MAVS locus with susceptibility to Addison's disease and type 1 diabetes
In the late phase of RNA viral infection, iRhom2 mediates proteasome-dependent degradation of the E3 ubiquitin ligase MARCH5 and impairs mitochondria-associated degradation (MAD) of VISA.
findings suggest that oxidative stress-induced MAVS oligomerization in SLE patients may contribute to the type I IFN signature that is characteristic of this syndrome.
findings reveal a negative feedback loop of RLR signaling generated by Tetherin-MARCH8-MAVS-NDP52 axis and provide insights into a better understanding of the crosstalk between selective autophagy and optimal deactivation of type I IFN signaling.
Studied association of genetic variants of the MAVS, MITA and MFN2 genes with leprosy in Han Chinese from Southwest China; found no association between the variants and susceptibility to leprosy.
Mechanistic studies showed that HACE1 exerts its inhibitory role on virus-induced signaling by disrupting the MAVS-TRAF3 complex.
this study shows that keratinocytes are an important source of IFN-beta and MAVS is critical to this function, and demonstrates how the epidermis triggers unwanted skin inflammation under disease conditions
Herpes simplex virus 1 blocks MAVS-Pex mediated early interferon-stimulated gene activation through VP16 to dampen the immediate early antiviral innate immunity signaling from peroxisomes.
This study demonstrates a novel pathway for elevated IFNbeta signaling in SLE that is not dependent on stimulation by immune complexes but rather is cell intrinsic and critically mediated by IFNbeta and MAVS.
These findings underscore MAVS as a vital innate immune system mediator in the intestinal mucosa and further suggests that MAVS-mediated maintenance of the intestinal epithelial barrier is an important defense against enteric pathogens.
Data show that interferon-beta promotor stimulator-1 (IPS-1) deficiency predisposed to severe pneumonia virus of mice (PVM) bronchiolitis.
MAVS deficiency is associated with allergic skin disease.
these data suggest that while MAVS signaling has a considerable impact on Treg identity, this effect is not mediated by intrinsic MAVS signaling but rather is likely an effect of the overproduction of pro-inflammatory cytokines generated in MAVS-deficient mice after WNV infection.
MAVS was identified as a main player in HDV detection and adaptive immunity was found to be involved in the amplification of the innate immune response.
MAVS is essential for spontaneous high basal expression of IFN-beta in cardiac myocytes and the heart.
RIPK3 regulates type I IFN both transcriptionally, by interacting with MAVS and limiting RIPK1 interaction with MAVS, and post-transcriptionally.
Data suggest that activation of either RIG-I/MAVS or STING pathways during acute intestinal tissue injury in mice resulted in IFN-I signaling that maintained gut epithelial barrier integrity and reduced GVHD severity.
this paper identifies TRIM31, an E3 ubiquitin ligase of the TRIM family of proteins, as a regulator of MAVS aggregation
Taken together, these results suggest that MAVS is essential for boosting optimal primary CD4(+) T cell responses upon NS4B-P38G West Nile virus vaccination and yet is dispensable for host protection and recall T cell responses during secondary wild-type West Nile virus infection.
this study demonstrates that the capacity of hepatitis A virus to evade MAVS-mediated type I interferon responses defines its host species range.
Hepatitis C virus NS3-4A inhibits the peroxisomal MAVS-dependent antiviral signaling response.
Rotavirus infection in macrophages depend on MAVS but not involve the NLRP3 inflammasome nor JNK and p38 signal pathway.
MARCH5 binds MAVS only during viral stimulation when MAVS forms aggregates, and these interactions require the RING domain of MARCH5 and the CARD domain of MAVS.
An autoinhibitory mechanism modulates MAVS activity in unstimulated cells and, on viral infection, individual regions of MAVS are released following MAVS filament formation to activate antiviral signalling cascades.
indicate comparable activation of the IFN response by pex- and mito-mitochondrial antiviral-signaling protein in hepatocytes and efficient counteraction of both MAVS species by the HCV nonstructural protein 3 protease
Transmembrane motif T6BM2-mediated TRAF6 binding is required for MAVS-related antiviral response.
Data show that intracellular adaptor protein Cardif-/- natural killer cells (NK cells) are more apoptotic and less proliferative.
upregulated at both the transcriptional and protein levels in the early stages of H3N2 infection
The authors determined that porcine reproductive and respiratory syndrome virus 3C protease cleaved MAVS at Glu268.
Real-time quantitative PCR analysis indicated that Tibetan porcine IPS-1 mRNA was most abundant in the liver and kidney.
Functions of the two zebrafish MAVS variants are opposite in the induction of IFN1 by targeting IRF7
Data show that mitochondrial antiviral signaling protein (MAVS) splicing variant 1 (MAVS_tv1) cooperated with DEAD (Asp-Glu-Ala-Asp) box polypeptide 58 RIG-I in the accumulation of RIG-I transcript in a positive feedback loop.
This gene encodes an intermediary protein necessary in the virus-triggered beta interferon signaling pathways. It is required for activation of transcription factors which regulate expression of beta interferon and contributes to antiviral immunity. Multiple transcript variants encoding different isoforms have been found for this gene.
CARD adapter inducing interferon beta
, CARD adaptor inducing IFN-beta
, IFN-B promoter stimulator 1
, interferon beta promoter stimulator protein 1
, mitochondrial antiviral-signaling protein
, putative NF-kappa-B-activating protein 031N
, virus-induced signaling adaptor
, virus-induced-signaling adapter
, virus-induced signaling adapter
, IFN-beta promoter stimulator-1
, mitochondrial anti-viral signaling protein
, mitochondrial IFN-beta promoter stimulator 1
, interferon-beta promoter stimulator protein 1