DEXH (Asp-Glu-X-His) Box Polypeptide 58 Proteins (DHX58)

Rainbow Trout (Oncorhynchus mykiss) DEXH (Asp-Glu-X-His) Box Polypeptide 58 (DHX58) interaction partners

1. MDA5 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.

Human DEXH (Asp-Glu-X-His) Box Polypeptide 58 (DHX58) interaction partners

1. Study demonstrated a tumor suppressor role of LGP2 in neuroblastoma (NB). LGP2 was effective in promoting poly (I:C)-induced NB suppression and cytoplasmic LGP2 can serve as an independent favorable prognostic factor in NB patients.

2. genetic loss of LGP2 uncovers dsRNA-mediated RNAi albeit less strongly than complete loss of the IFN system

3. Results indicate that pumilio RNA binding family member 1 (PUM1) is a negative regulator of RNA helicase LGP2 (LGP2), a master regulator of innate immunity genes expressed in a cascade fashion.

4. study documents that recombinant measles virus produce defective interfering genomes that have high immunostimulatory properties via their binding to RIG-I and LGP2 proteins, both of which are cytosolic nonself RNA sensors of innate immunity.

5. Data support a new model where an LGP2-MDA5 oligomer shuttles NS3 to the mitochondria to block antiviral signaling

6. essential role in activating interferon signaling against hepatitis C virus (HCV) infection by promoting MDA5 recognition of HCV pathogen-associated molecular patterns

7. This review briefly summarizes the RLR system, and focuses on the relationship between LGP2 and MDA5, describing in detail how these two proteins work together to detect foreign RNA and generate a fully functional antiviral response.

8. 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 in virally-infected cells.

9. LGP2 did not reveal significant single-SNP associations with multiple sclerosis risk.

10. LGP2 increases the initial rate of MDA5-RNA interaction and regulates MDA5 filament assembly.

11. Experiments with paramyxovirus V protein-insensitive proteins revealed that the primary outcome of LGP2 interference is suppression of its ability to synergize with MDA5.

12. Data show that LGP2 is able to synergize with melanoma differentiation associated gene-5 (mda-5) to render cells to induction by poly(I:C), but did not enhance retinoic acid-inducible gene-I (RIG-I) to induce type I interferon in response to poly(I:C).

13. results demonstrate previously unrecognized properties of LGP2 ATP hydrolysis and RNA interaction and provide a mechanistic basis for a positive regulatory role for LGP2 in antiviral signaling

14. LGP2, a host protein induced during influenza A virus infection, downregulates the host antiviral IFN response

15. Paramyxovirus 5 V proteins interact with the RNA Helicase LGP2 to inhibit RIG-I-dependent interferon beta induction.

16. the present study shows the presence of RIG-1,MDA-5, and LGP-2 in the human upper airways, most prominently inthe epithelium.

17. LGP2 functions as an inhibitor of the innate immune response triggered by Rabeis virus infection

18. Data sugget that DeltaPsi(m) and MAVS are coupled at the same stage in the RLR antiviral signaling pathway.

19. Shared and unique functions of the DExD/H-box helicases RIG-I, MDA5, and LGP2 in antiviral innate immunity.

20. LGP2 competes with the kinase IKKi for a common interaction site on IPS-1, as an element of negative-feedback regulation of intracellular antiviral signaling.

Mouse (Murine) DEXH (Asp-Glu-X-His) Box Polypeptide 58 (DHX58) interaction partners

1. 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.

2. 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 in virally-infected cells.

3. This in vivo study reveals that LGP2 is a major downregulator of the influenza A virus-triggered detrimental inflammatory response.

4. Enhanced expression of LGP2 suppresses the IFN stimulated genes associated with cytotoxic stress by turning off the expression of IFNbeta

5. LGP2, a host protein induced during influenza A virus infection, downregulates the host antiviral IFN response

6. LGP2 promotes an essential prosurvival signal in response to antigen stimulation to confer CD8+ T cell-number expansion and effector functions against divergent RNA viruses, including West Nile virus and lymphocytic choriomeningitis virus.

7. 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

8. data suggest that LGP2 facilitates viral RNA recognition by RIG-I and MDA5 through its ATPase domain.

9. Lgp2 acts as a negative feedback regulator of antiviral signaling by sequestering double-stranded RNA from retinoic acid-inducible gene-I (RIG-I).

10. Functional analysis of the human LGP2 ortholog.

Pig (Porcine) DEXH (Asp-Glu-X-His) Box Polypeptide 58 (DHX58) interaction partners

1. Study indicates that DHX58 is an important gene that is associated with the immune response in swine.

Cow (Bovine) DEXH (Asp-Glu-X-His) Box Polypeptide 58 (DHX58) interaction partners

1. Functional analysis of the human LGP2 ortholog.