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Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling.
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MDA5 (show IFIH1 Proteins) and LGP2 act as independent positive regulators of the IFN response in fish. the LGP2 variant with a deletion of 54 amino acids at the C terminus acts as a negative regulator for LGP2-elicited antiviral signaling.
Results indicate that pumilio RNA binding family member 1 (PUM1 (show PUM1 Proteins)) is a negative regulator of RNA helicase LGP2 (LGP2), a master regulator of innate immunity genes expressed in a cascade fashion.
study documents that recombinant measles virus produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I (show DDX58 Proteins) and LGP2 proteins, both of which are cytosolic nonself RNA sensors of innate immunity.
Data support a new model where an LGP2-MDA5 oligomer shuttles NS3 to the mitochondria to block antiviral signaling
essential role in activating interferon (show IFNA Proteins) signaling against hepatitis C virus (HCV) infection by promoting MDA5 (show IFIH1 Proteins) recognition of HCV pathogen-associated molecular patterns
This review briefly summarizes the RLR system, and focuses on the relationship between LGP2 and MDA5 (show IFIH1 Proteins), describing in detail how these two proteins work together to detect foreign RNA and generate a fully functional antiviral response.
L region antisense RNA of EMCV is a key determinant of innate immunity to the virus and represents an RNA that activates LGP2 associated MDA5 (show IFIH1 Proteins) in virally-infected cells.
LGP2 did not reveal significant single-SNP associations with multiple sclerosis risk.
LGP2 increases the initial rate of MDA5 (show IFIH1 Proteins)-RNA interaction and regulates MDA5 (show IFIH1 Proteins) filament assembly.
Experiments with paramyxovirus V protein-insensitive proteins revealed that the primary outcome of LGP2 interference is suppression of its ability to synergize with MDA5 (show IFIH1 Proteins).
Data show that LGP2 is able to synergize with melanoma differentiation associated gene-5 (mda-5 (show IFIH1 Proteins)) to render cells to induction by poly(I:C), but did not enhance retinoic acid-inducible gene-I (RIG-I (show DDX58 Proteins)) to induce type I interferon (show IFNA Proteins) in response to poly(I:C).
PACT interacts with LGP2 and this interaction is enhanced by encephalomyocarditis virus (EMCV) infection. In vitro interaction analyses using purified recombinant proteins confirmed that the single-stranded Theiler's murine encephalitis virus genome enhanced the interaction between LGP2 and PACT.
This in vivo study reveals that LGP2 is a major downregulator of the influenza A virus-triggered detrimental inflammatory response.
Enhanced expression of LGP2 suppresses the IFN stimulated genes associated with cytotoxic stress by turning off the expression of IFNbeta
LGP2, a host protein induced during influenza A virus infection, downregulates the host antiviral IFN response
LGP2 promotes an essential prosurvival signal in response to antigen stimulation to confer CD8 (show CD8A Proteins)+ T cell-number expansion and effector functions against divergent RNA viruses, including West Nile virus and lymphocytic choriomeningitis virus.
findings demonstrate a regulatory role for LGP2 in the response to cytosolic DNA, an intracellular bacterial pathogen, and a DNA virus, and provide a plausible mechanistic hypothesis as the basis for this activity
data suggest that LGP2 facilitates viral RNA recognition by RIG-I and MDA5 through its ATPase domain.
Lgp2 acts as a negative feedback regulator of antiviral signaling by sequestering double-stranded RNA from retinoic acid-inducible gene-I (RIG-I (show DDX58 Proteins)).
Functional analysis of the human LGP2 ortholog.
Study indicates that DHX58 is an important gene that is associated with the immune response in swine.
Acts as a regulator of DDX58/RIG-I and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1- dependent signaling events. Can have both negative and positive regulatory functions related to DDX58/RIG-I and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on DDX58/RIG-I DDX58/RIG-I for binding to the viral RNA, binding to DDX58/RIG-I and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by DDX58/RIG-I and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.
DEXH (Asp-Glu-X-His) box polypeptide 58
, probable ATP-dependent RNA helicase DHX58
, probable ATP-dependent RNA helicase DHX58-like
, Probable ATP-dependent RNA helicase DHX58
, RIG-I-like receptor 3
, RIG-I-like receptor LGP2
, RNA helicase LGP2
, ortholog of mouse D11lgp2
, probable ATP-dependent helicase LGP2
, protein D11Lgp2 homolog
, RIG-I-like receptor Lgp2
, protein D11Lgp2
, ATP-dependent RNA helicase DHX58