Molecular characterization, expression patterns, and subcellular localization of RIG-I in the Jinding Duck (Anas platyrhynchos domesticus)

Chen, Yang; Zhang, Yang; Huang, Zheng; Xu, Qi; Zhu, Zhen; Tong, Yiyu; Yu, Qinmin; Ding, Jun; Chen, Guohong

doi:10.1016/j.dci.2013.07.018

Cited by 16 publications

(9 citation statements)

References 25 publications

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“…We previously reported expression of duRIG-I increased in spleen and liver after poly[I:C] challenge [ 14 ]. Also, Barber et al and Huang et al proposed that duRIG-I deletion might underlie the sensitivity of chicken to avian influenza [ 15 , 16 ].…”

Section: Introductionmentioning

confidence: 99%

Duck RIG-I CARD Domain Induces the Chicken IFN-βby Activating NF-κB

Chen

Huang

Wang

et al. 2015

BioMed Research International

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Retinoic acid-inducible gene I- (RIG-I-) like receptors (RLRs) have recently been identified as cytoplasmic sensors for viral RNA. RIG-I, a member of RLRs family, plays an important role in innate immunity. Although previous investigations have proved that RIG-I is absent in chickens, it remains largely unknown whether the chicken can respond to RIG-I ligand. In this study, the eukaryotic expression vectors encoding duRIG-I full length (duck RIG-I, containing all domains), duRIG-I N-terminal (containing the two caspase activation and recruitment domain, CARDs), and duRIG-I C-terminal (containing helicase and regulatory domains) labeled with 6∗His tags were constructed successfully and detected by western blotting. Luciferase reporter assay and enzyme-linked immunosorbent assay (ELISA) detected the duRIG-I significantly activated NF-κB and induced the expression of IFN-β when polyinosinic-polycytidylic acid (poly[I:C], synthetic double-stranded RNA) challenges chicken embryonic fibroblasts cells (DF1 cells), while the duRIG-I was inactive in the absence of poly[I:C]. Further analysis revealed that the CARDs (duRIG-I-N) induced IFN-β production regardless of the presence of poly[I:C], while the CARD-lacking duRIG-I (duRIG-I-C) was not capable of activating downstream signals. These results indicate that duRIG-I CARD domain plays an important role in the induction of IFN-β and provide a basis for further studying the function of RIG-I in avian innate immunity.

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Section: Introductionmentioning

confidence: 99%

Duck RIG-I CARD Domain Induces the Chicken IFN-βby Activating NF-κB

Chen

Huang

Wang

et al. 2015

BioMed Research International

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“…Poly (I:C) is nontoxic or lentogenic to duck, so the rapid return to basal level of duIFIT5 expression might be because ducklings have a relatively high resistance to poly (I:C). Besides, our previous study have shown that duck RIG-I gene had a similar expression pattern after poly (I:C) infection[ 28 ]. RIG-I is considered to be a upstream gene for IFITs[ 29 , 30 ], so the result could also demonstrate that duck RIG-I and IFIT5 are well connected.…”

Section: Discussionmentioning

confidence: 99%

Identification and Expression Analysis of the Interferon-Induced Protein with Tetratricopeptide Repeats 5 (IFIT5) Gene in Duck (Anas platyrhynchos domesticus)

Wang

Chen

et al. 2015

PLoS ONE

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The interferon-induced proteins with tetratricopeptide repeats (IFITs) protein family mediates antiviral effects by inhibiting translation initiation, cell proliferation, and migration in the interferon (IFN) dependent innate immune system. Several members of this family, including IFIT1, IFIT2, IFIT3 and IFIT5, have been heavily studied in mammals. Avian species contain only one family member, IFIT5, and little is known about the role of this protein in birds. In this study, duck IFIT5 (duIFIT5) full-length mRNA was cloned by reverse transcription polymerase chain reaction (RT-PCR) and rapid amplification of the cDNA ends (RACE). Based on the sequence obtained, we performed a series of bioinformatics analyses, and found that duIFIT5 was most similar to homologs in other avian species. Also, duIFIT5 contained eight conserved TPR motifs and two conserved multi-domains (TPR_11 and TPR_12). Finally, we used duck hepatitis virus type 1 (DHV-1) and polyriboinosinicpolyribocytidylic acid (poly (I:C)) as a pathogen or a pathogen-associated molecular pattern induction to infect three-day-old domestic ducklings. The liver and spleen were collected to detect the change in duIFIT5 transcript level upon infection by quantitative real-time PCR (qRT-PCR). DuIFIT5 expression rapidly increased after DHV-1 infection and maintained a high level, while the transcripts of duIFIT5 peaked at 8h after poly (I:C) infection and then returned to normal. Taken together, these results provide a greater understanding of avian IFIT5.

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“…pCAGGS-HA expression plasmids encoding truncated duTRAF3 fragments, including HA-T31-216, HA-T321, HA-T3319, HA-Δcoil3, and HA-TRAF-C-domain, were obtained by PCR amplification of HA-duTRAF3. Based on the previous studies ( 22 – 25 ), duRIG-I, duRIG-I(N), duMDA5(N), duMAVS, and duTRIF were amplified from duck cDNA and cloned into the p3xFlag-CMV-14 vector with C -terminal Flag epitope tags. Flag-tagged duTLR3 was kindly provided by Dr. Peirong Jiao (Huanan Agricultural University).…”

Section: Methodsmentioning

confidence: 99%

Negative Regulation of Interferon-β Production by Alternative Splicing of Tumor Necrosis Factor Receptor-Associated Factor 3 in Ducks

Wei

Qian

Sizhu³

et al. 2018

Front. Immunol.

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Tumor necrosis factor receptor-associated factor 3 (TRAF3), an intracellular signal transducer, is identified as an important component of Toll-like receptors and RIG-I-like receptors induced type I interferon (IFN) signaling pathways. Previous studies have clarified TRAF3 function in mammals, but little is known about the role of TRAF3 in ducks. Here, we cloned and characterized the full-length duck TRAF3 (duTRAF3) gene and an alternatively spliced isoform of duTRAF3 (duTRAF3-S) lacking the fragment encoding amino acids 217–319, from duck embryo fibroblasts (DEFs). We found that duTRAF3 and duTRAF3-S played different roles in regulating IFN-β production in DEFs. duTRAF3 through its TRAF domain interacted with duMAVS or duTRIF, leading to the production of IFN-β. However, duTRAF3-S, containing the TRAF domain, was unable to bind duMAVS or duTRIF due to the intramolecular binding between the N- and C-terminal of duTRAF3-S that blocked the function of its TRAF domain. Further analysis identified that duTRAF3-S competed with duTRAF3 itself for binding to duTRAF3, perturbing duTRAF3 self-association, which impaired the assembly of duTRAF3-duMAVS/duTRIF complex, ultimately resulted in a reduced production of IFN-β. These findings suggest that duTRAF3 is an important regulator of duck innate immune signaling and reveal a novel mechanism for the negative regulation of IFN-β production via changing the formation of the homo-oligomerization of wild molecules, implying a novel regulatory role of truncated proteins.

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Molecular characterization, expression patterns, and subcellular localization of RIG-I in the Jinding Duck (Anas platyrhynchos domesticus)

Cited by 16 publications

References 25 publications

Duck RIG-I CARD Domain Induces the Chicken IFN-βby Activating NF-κB

Duck RIG-I CARD Domain Induces the Chicken IFN-βby Activating NF-κB

Identification and Expression Analysis of the Interferon-Induced Protein with Tetratricopeptide Repeats 5 (IFIT5) Gene in Duck (Anas platyrhynchos domesticus)

Negative Regulation of Interferon-β Production by Alternative Splicing of Tumor Necrosis Factor Receptor-Associated Factor 3 in Ducks

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