Expression of immune genes RIG-I and Mx in mallard ducks infected with low pathogenic avian influenza (LPAI): A dataset

Helin, Anu S.; Wille, Michelle; Atterby, Clara; Järhult, Josef D.; Waldenström, Jonas; Chapman, J. R.

doi:10.1016/j.dib.2018.04.061

Cited by 3 publications

(3 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…24,38,173 Moreover, RIG-I orthologues in birds and fish have been shown to play a key role in producing an IFN response to viral infections, indicating that the function of RIG-I is also conserved across species. [166][167][168][169][170][171][172] Altogether, structural and cellular studies of RIG-I…”

Section: Ri G -I S I G Naling Is Con S Erved Among D Ifferent S Pecie Smentioning

confidence: 99%

“… 165 While closely related RIG‐I othologues are found in all mammals, in other vertebrates, conservation of RIG‐I is more limited. 166 , 167 , 168 , 169 , 170 , 171 , 172 Protein sequence alignment of RIG‐I among mammals, birds, and fish reveals that the domain organization of RIG‐I is similar in these classes, and that the key residues involved in RNA recognition, ATP binding, and hydrolysis are all conserved (Figure 3 ). Furthermore, crystal structures of truncated human, mouse, and duck RIG‐I constructs reveal a highly conserved architecture of RIG‐I, particularly the key residues in the RNA binding pocket of the CTD (H847, K858, K861, and K888) and in the catalytic core of the ATPase domain (K270).…”

Section: Rig‐i Signaling Is Conserved Among Different Speciesmentioning

confidence: 99%

“… 24 , 38 , 173 Moreover, RIG‐I orthologues in birds and fish have been shown to play a key role in producing an IFN response to viral infections, indicating that the function of RIG‐I is also conserved across species. 166 , 167 , 168 , 169 , 170 , 171 , 172 Altogether, structural and cellular studies of RIG‐I orthologues reveal conserved RIG‐I structure and function across many classes of vertebrates, suggesting that in species where the RIG‐I gene is retained, its essential function in responding to viral infections is also conserved.…”

Section: Rig‐i Signaling Is Conserved Among Different Speciesmentioning

confidence: 99%

See 2 more Smart Citations

The molecular mechanism of RIG‐I activation and signaling

Thoresen

Wang

Galls

et al. 2021

Immunological Reviews

132

View full text Add to dashboard Cite

One of the most important cellular defenses against RNA viruses is a large, multidomain protein known as RIG-I (Retinoic Acid Inducible Gene I), which functions as a pattern recognition receptor (PRR) that triggers early innate immune responses in vertebrate cells. 1-3 RIG-I is a member of a conserved family of double-stranded RNA (dsRNA) binding proteins that includes additional innate immune surveillance proteins MDA5 and LGP2. [3][4][5] By recognizing and responding to different types of viral RNA motifs, this family (known as the RIG-I-like receptors or RLRs) provides broad protection against viral infections. These proteins are, in turn, closely related to members of the broader Dicer family, such as DRH3 (Dicer related helicase 3), as all of these proteins share a distinctive set of dsRNA binding domains, and an ATPase core that is catalytically activated only upon binding of dsRNA. 6,7 This link between RLRs and Dicer-like proteins involved in miRNA processing suggests a shared evolutionary heritage and the possibility of cross-talk between these two systems. 5 The helicase core of the RLR/Dicer family proteins (previously termed DRAs) is distinct, 7 but identifiable as a member of Helicase Superfamily 2

show abstract

Section: Ri G -I S I G Naling Is Con S Erved Among D Ifferent S Pecie Smentioning

confidence: 99%

Section: Rig‐i Signaling Is Conserved Among Different Speciesmentioning

confidence: 99%

Section: Rig‐i Signaling Is Conserved Among Different Speciesmentioning

confidence: 99%

See 1 more Smart Citation

The molecular mechanism of RIG‐I activation and signaling

Thoresen

Wang

Galls

et al. 2021

Immunological Reviews

132

View full text Add to dashboard Cite

show abstract

A rapid and transient innate immune response to avian influenza infection in mallards

Helin

Wille

Atterby

et al. 2018

Molecular Immunology

View full text Add to dashboard Cite

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

2019

View full text Add to dashboard Cite

RIG-I (Retinoic acid-inducible gene I) and MDA5 (Melanoma Differentiation-Associated protein 5), collectively known as the RIG-I-like receptors (RLRs), are key protein sensors of the pathogen-associated molecular patterns (PAMPs) in the form of viral double-stranded RNA (dsRNA) motifs to induce expression of type 1 interferons (IFN1) (IFNα and IFNβ) and other pro-inflammatory cytokines during the early stage of viral infection. While RIG-I and MDA5 share many genetic, structural and functional similarities, there is increasing evidence that they can have significantly different strategies to recognize different pathogens, PAMPs, and in different host species. This review article discusses the similarities and differences between RIG-I and MDA5 from multiple perspectives, including their structures, evolution and functional relationships with other cellular proteins, their differential mechanisms of distinguishing between host and viral dsRNAs and interactions with host and viral protein factors, and their immunogenic signaling. A comprehensive comparative analysis can help inform future studies of RIG-I and MDA5 in order to fully understand their functions in order to optimize potential therapeutic approaches targeting them.

show abstract

Expression of immune genes RIG-I and Mx in mallard ducks infected with low pathogenic avian influenza (LPAI): A dataset

Cited by 3 publications

References 15 publications

The molecular mechanism of RIG‐I activation and signaling

The molecular mechanism of RIG‐I activation and signaling

A rapid and transient innate immune response to avian influenza infection in mallards

Comparative Structure and Function Analysis of the RIG-I-Like Receptors: RIG-I and MDA5

Contact Info

Product

Resources

About