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Article ; Online: Correction: CBAP regulates the function of Akt-associated TSC protein complexes to modulate mTORC1 signaling.

Liao, Wei-Ting / Chiang, Yun-Jung / Yang-Yen, Hsin-Fang / Hsu, Li-Chung / Chang, Zee-Fen / Yen, Jeffrey J Y

2024 Volume 300, Issue 2, Page(s) 105686

Language	English
Publishing date	2024-01-29
Publishing country	United States
Document type	Published Erratum
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.105686
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Article ; Online: CBAP regulates the function of Akt-associated TSC protein complexes to modulate mTORC1 signaling.

Liao, Wei-Ting / Chiang, Yun-Jung / Yang-Yen, Hsin-Fang / Hsu, Li-Chung / Chang, Zee-Fen / Yen, Jeffrey J Y

The Journal of biological chemistry

2023 Volume 299, Issue 12, Page(s) 105455

Abstract: The Akt-Rheb-mTORC1 pathway plays a crucial role in regulating cell growth, but the mechanisms underlying the activation of Rheb-mTORC1 by Akt remain unclear. In our previous study, we found that CBAP was highly expressed in human T-ALL cells and primary ...

Abstract	The Akt-Rheb-mTORC1 pathway plays a crucial role in regulating cell growth, but the mechanisms underlying the activation of Rheb-mTORC1 by Akt remain unclear. In our previous study, we found that CBAP was highly expressed in human T-ALL cells and primary tumors, and its deficiency led to reduced phosphorylation of TSC2/S6K1 signaling proteins as well as impaired cell proliferation and leukemogenicity. We also demonstrated that CBAP was required for Akt-mediated TSC2 phosphorylation in vitro. In response to insulin, CBAP was also necessary for the phosphorylation of TSC2/S6K1 and the dissociation of TSC2 from the lysosomal membrane. Here we report that CBAP interacts with AKT and TSC2, and knockout of CBAP or serum starvation leads to an increase in TSC1 in the Akt/TSC2 immunoprecipitation complexes. Lysosomal-anchored CBAP was found to override serum starvation and promote S6K1 and 4EBP1 phosphorylation and c-Myc expression in a TSC2-dependent manner. Additionally, recombinant CBAP inhibited the GAP activity of TSC2 complexes in vitro, leading to increased Rheb-GTP loading, likely due to the competition between TSC1 and CBAP for binding to the HBD domain of TSC2. Overexpression of the N26 region of CBAP, which is crucial for binding to TSC2, resulted in a decrease in mTORC1 signaling and an increase in TSC1 association with the TSC2/AKT complex, ultimately leading to increased GAP activity toward Rheb and impaired cell proliferation. Thus, we propose that CBAP can modulate the stability of TSC1-TSC2 as well as promote the translocation of TSC1/TSC2 complexes away from lysosomes to regulate Rheb-mTORC1 signaling.
MeSH term(s)	Humans ; Cell Proliferation ; Guanosine Triphosphate/metabolism ; Immunoprecipitation ; Lysosomes/metabolism ; Mechanistic Target of Rapamycin Complex 1/metabolism ; Membrane Proteins/deficiency ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-akt/metabolism ; Ras Homolog Enriched in Brain Protein/metabolism ; TOR Serine-Threonine Kinases/metabolism ; Tuberous Sclerosis Complex 1 Protein/metabolism ; Tuberous Sclerosis Complex 2 Protein/metabolism
Chemical Substances	Guanosine Triphosphate (86-01-1) ; Mechanistic Target of Rapamycin Complex 1 (EC 2.7.11.1) ; Membrane Proteins ; MYC protein, human ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Ras Homolog Enriched in Brain Protein ; RHEB protein, human ; ribosomal protein S6 kinase, 70kD, polypeptide 1 (EC 2.7.11.1) ; TMEM102 protein, human ; TOR Serine-Threonine Kinases (EC 2.7.11.1) ; TSC1 protein, human ; TSC2 protein, human ; Tuberous Sclerosis Complex 1 Protein ; Tuberous Sclerosis Complex 2 Protein
Language	English
Publishing date	2023-11-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2023.105455
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Article: Therapeutic Development Based on the Immunopathogenic Mechanisms of Psoriasis.

Tseng, Jen-Chih / Chang, Yung-Chi / Huang, Chun-Ming / Hsu, Li-Chung / Chuang, Tsung-Hsien

Pharmaceutics

2021 Volume 13, Issue 7

Abstract: Psoriasis, a complex inflammatory autoimmune skin disorder that affects 2-3% of the global population, is thought to be genetically predetermined and induced by environmental and immunological factors. In the past decades, basic and clinical studies have ...

Abstract	Psoriasis, a complex inflammatory autoimmune skin disorder that affects 2-3% of the global population, is thought to be genetically predetermined and induced by environmental and immunological factors. In the past decades, basic and clinical studies have significantly expanded knowledge on the molecular, cellular, and immunological mechanisms underlying the pathogenesis of psoriasis. Based on these pathogenic mechanisms, the current disease model emphasizes the role of aberrant Th1 and Th17 responses. Th1 and Th17 immune responses are regulated by a complex network of different cytokines, including TNF-α, IL-17, and IL-23; signal transduction pathways downstream to the cytokine receptors; and various activated transcription factors, including NF-κB, interferon regulatory factors (IRFs), and signal transducer and activator of transcriptions (STATs). The biologics developed to specifically target the cytokines have achieved a better efficacy and safety for the systemic management of psoriasis compared with traditional treatments. Nevertheless, the current therapeutics can only alleviate the symptoms; there is still no cure for psoriasis. Therefore, the development of more effective, safe, and affordable therapeutics for psoriasis is important. In this review, we discussed the current trend of therapeutic development for psoriasis based on the recent discoveries in the immune modulation of the inflammatory response in psoriasis.
Language	English
Publishing date	2021-07-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527217-2
ISSN	1999-4923
ISSN	1999-4923
DOI	10.3390/pharmaceutics13071064
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Article ; Online: K48/K63-linked polyubiquitination of ATG9A by TRAF6 E3 ligase regulates oxidative stress-induced autophagy.

Wang, Yi-Ting / Liu, Ting-Yu / Shen, Chia-Hsing / Lin, Shu-Yu / Hung, Chin-Chun / Hsu, Li-Chung / Chen, Guang-Chao

Cell reports

2022 Volume 38, Issue 8, Page(s) 110354

Abstract: Excessive generation and accumulation of highly reactive oxidizing molecules causes oxidative stress and oxidative damage to cellular components. Accumulating evidence indicates that autophagy diminishes oxidative damage in cells and maintains redox ... ...

Abstract	Excessive generation and accumulation of highly reactive oxidizing molecules causes oxidative stress and oxidative damage to cellular components. Accumulating evidence indicates that autophagy diminishes oxidative damage in cells and maintains redox homeostasis by degrading and recycling intracellular damaged components. Here, we show that TRAF6 E3 ubiquitin ligase and A20 deubiquitinase coordinate to regulate ATG9A ubiquitination and autophagy activation in cells responding to oxidative stress. The ROS-dependent TRAF6-mediated non-proteolytic, K48/63-linked ubiquitination of ATG9A enhances its association with Beclin 1 and the assembly of VPS34-UVRAG complex, thereby stimulating autophagy. Notably, expression of the ATG9A ubiquitination mutants impairs ROS-induced VPS34 activation and autophagy. We further find that lipopolysaccharide (LPS)-induced ROS production also stimulates TRAF6-mediated ATG9A ubiquitination. Ablation of ATG9A causes aberrant TLR4 endosomal trafficking and decreases IRF-3 phosphorylation in LPS-stimulated macrophages. Our findings provide important insights into how K48/K63-linked ubiquitination of ATG9A contributes to the regulation of oxidative stress-induced autophagy.
MeSH term(s)	Autophagy/physiology ; Oxidative Stress ; TNF Receptor-Associated Factor 6/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	TNF Receptor-Associated Factor 6 ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2022-02-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.110354
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Article ; Online: TLR9 and STING agonists cooperatively boost the immune response to SARS-CoV-2 RBD vaccine through an increased germinal center B cell response and reshaped T helper responses.

Yang, Jing-Xing / Tseng, Jen-Chih / Tien, Chih-Feng / Lee, Chia-Yin / Liu, Yi-Ling / Lin, Jhe-Jhih / Tsai, Pei-Ju / Liao, Hung-Chun / Liu, Shih-Jen / Su, Yu-Wen / Hsu, Li-Chung / Chen, Jen-Kun / Huang, Ming-Hsi / Yu, Guann-Yi / Chuang, Tsung-Hsien

International journal of biological sciences

2023 Volume 19, Issue 9, Page(s) 2897–2913

Abstract: Vaccines are a powerful medical intervention for preventing epidemic diseases. Efficient inactivated or protein vaccines typically rely on an effective adjuvant to elicit an immune response and boost vaccine activity. In this study, we investigated the ... ...

Abstract	Vaccines are a powerful medical intervention for preventing epidemic diseases. Efficient inactivated or protein vaccines typically rely on an effective adjuvant to elicit an immune response and boost vaccine activity. In this study, we investigated the adjuvant activities of combinations of Toll-like receptor 9 (TLR9) and stimulator of interferon genes (STING) agonists in a SARS-CoV-2 receptor binding domain protein vaccine. Adjuvants formulated with a TLR9 agonist, CpG-2722, with various cyclic dinucleotides (CDNs) that are STING agonists increased germinal center B cell response and elicited humoral immune responses in immunized mice. An adjuvant containing CpG-2722 and 2'3'-c-di-AM(PS)2 effectively boosted the immune response to both intramuscularly and intranasally administrated vaccines. Vaccines adjuvanted with CpG-2722 or 2'3'-c-di-AM(PS)2 alone were capable of inducing an immune response, but a cooperative adjuvant effect was observed when both were combined. CpG-2722 induced antigen-dependent T helper (Th)1 and Th17 responses, while 2'3'-c-di-AM(PS)2 induced a Th2 response. The combination of CpG-2722 and 2'3'-c-di-AM(PS)2 generated a distinct antigen-dependent Th response profile characterized by higher Th1 and Th17, but lower Th2 responses. In dendritic cells, CpG-2722 and 2'3'-c-di-AM(PS)2 showed a cooperative effect on inducing expression of molecules critical for T cell activation. CpG-2722 and 2'3'-c-di-AM(PS)2 have distinct cytokine inducing profiles in different cell populations. The combination of these two agonists enhanced the expression of cytokines for Th1 and Th17 responses and suppressed the expression of cytokines for Th2 response in these cells. Thus, the antigen-dependent Th responses observed in the animals immunized with different vaccines were shaped by the antigen-independent cytokine-inducing profiles of their adjuvant. The expanded targeting cell populations, the increased germinal center B cell response, and reshaped T helper responses are the molecular bases for the cooperative adjuvant effect of the combination of TLR9 and STING agonists.
MeSH term(s)	Animals ; Mice ; COVID-19 Vaccines ; Toll-Like Receptor 9/agonists ; SARS-CoV-2 ; Oligodeoxyribonucleotides/pharmacology ; COVID-19 ; Adjuvants, Immunologic/pharmacology ; Adjuvants, Immunologic/chemistry ; Cytokines ; Vaccines ; Immunity ; Germinal Center
Chemical Substances	COVID-19 Vaccines ; Toll-Like Receptor 9 ; Oligodeoxyribonucleotides ; Adjuvants, Immunologic ; Cytokines ; Vaccines
Language	English
Publishing date	2023-05-29
Publishing country	Australia
Document type	Journal Article
ZDB-ID	2179208-2
ISSN	1449-2288 ; 1449-2288
ISSN (online)	1449-2288
ISSN	1449-2288
DOI	10.7150/ijbs.81210
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Article ; Online: The Src-ZNRF1 axis controls TLR3 trafficking and interferon responses to limit lung barrier damage.

Lin, You-Sheng / Chang, Yung-Chi / Chao, Tai-Ling / Tsai, Ya-Min / Jhuang, Shu-Jhen / Ho, Yu-Hsin / Lai, Ting-Yu / Liu, Yi-Ling / Chen, Chiung-Ya / Tsai, Ching-Yen / Hsueh, Yi-Ping / Chang, Sui-Yuan / Chuang, Tsung-Hsien / Lee, Chih-Yuan / Hsu, Li-Chung

The Journal of experimental medicine

2023 Volume 220, Issue 8

Abstract: Type I interferons are important antiviral cytokines, but prolonged interferon production is detrimental to the host. The TLR3-driven immune response is crucial for mammalian antiviral immunity, and its intracellular localization determines induction of ... ...

Abstract	Type I interferons are important antiviral cytokines, but prolonged interferon production is detrimental to the host. The TLR3-driven immune response is crucial for mammalian antiviral immunity, and its intracellular localization determines induction of type I interferons; however, the mechanism terminating TLR3 signaling remains obscure. Here, we show that the E3 ubiquitin ligase ZNRF1 controls TLR3 sorting into multivesicular bodies/lysosomes to terminate signaling and type I interferon production. Mechanistically, c-Src kinase activated by TLR3 engagement phosphorylates ZNRF1 at tyrosine 103, which mediates K63-linked ubiquitination of TLR3 at lysine 813 and promotes TLR3 lysosomal trafficking and degradation. ZNRF1-deficient mice and cells are resistant to infection by encephalomyocarditis virus and SARS-CoV-2 because of enhanced type I interferon production. However, Znrf1-/- mice have exacerbated lung barrier damage triggered by antiviral immunity, leading to enhanced susceptibility to respiratory bacterial superinfections. Our study highlights the c-Src-ZNRF1 axis as a negative feedback mechanism controlling TLR3 trafficking and the termination of TLR3 signaling.
MeSH term(s)	Animals ; Mice ; Antiviral Agents ; COVID-19 ; Interferon Type I ; SARS-CoV-2 ; Toll-Like Receptor 3 ; Genes, src
Chemical Substances	Antiviral Agents ; Interferon Type I ; TLR3 protein, mouse ; Toll-Like Receptor 3 ; ZNRF1 protein, mouse (EC 2.3.2.27)
Language	English
Publishing date	2023-05-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20220727
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Article: ZNRF1 Mediates Epidermal Growth Factor Receptor Ubiquitination to Control Receptor Lysosomal Trafficking and Degradation.

Shen, Chia-Hsing / Chou, Chih-Chang / Lai, Ting-Yu / Hsu, Jer-En / Lin, You-Sheng / Liu, Huai-Yu / Chen, Yan-Kai / Ho, I-Lin / Hsu, Pang-Hung / Chuang, Tsung-Hsien / Lee, Chih-Yuan / Hsu, Li-Chung

Frontiers in cell and developmental biology

2021 Volume 9, Page(s) 642625

Abstract: Activation of the epidermal growth factor receptor (EGFR) is crucial for development, tissue homeostasis, and immunity. Dysregulation of EGFR signaling is associated with numerous diseases. EGFR ubiquitination and endosomal trafficking are key events ... ...

Abstract	Activation of the epidermal growth factor receptor (EGFR) is crucial for development, tissue homeostasis, and immunity. Dysregulation of EGFR signaling is associated with numerous diseases. EGFR ubiquitination and endosomal trafficking are key events that regulate the termination of EGFR signaling, but their underlying mechanisms remain obscure. Here, we reveal that ZNRF1, an E3 ubiquitin ligase, controls ligand-induced EGFR signaling via mediating receptor ubiquitination. Deletion of ZNRF1 inhibits endosome-to-lysosome sorting of EGFR, resulting in delayed receptor degradation and prolonged downstream signaling. We further demonstrate that ZNRF1 and Casitas B-lineage lymphoma (CBL), another E3 ubiquitin ligase responsible for EGFR ubiquitination, mediate ubiquitination at distinct lysine residues on EGFR. Furthermore, loss of ZNRF1 results in increased susceptibility to herpes simplex virus 1 (HSV-1) infection due to enhanced EGFR-dependent viral entry. Our findings identify ZNRF1 as a novel regulator of EGFR signaling, which together with CBL controls ligand-induced EGFR ubiquitination and lysosomal trafficking.
Language	English
Publishing date	2021-04-29
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2737824-X
ISSN	2296-634X
ISSN	2296-634X
DOI	10.3389/fcell.2021.642625
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Article ; Online: Terminal uridyltransferase 7 regulates TLR4-triggered inflammation by controlling Regnase-1 mRNA uridylation and degradation.

Lin, Chia-Ching / Shen, Yi-Ru / Chang, Chi-Chih / Guo, Xiang-Yi / Young, Yun-Yun / Lai, Ting-Yu / Yu, I-Shing / Lee, Chih-Yuan / Chuang, Tsung-Hsien / Tsai, Hsin-Yue / Hsu, Li-Chung

Nature communications

2021 Volume 12, Issue 1, Page(s) 3878

Abstract: Different levels of regulatory mechanisms, including posttranscriptional regulation, are needed to elaborately regulate inflammatory responses to prevent harmful effects. Terminal uridyltransferase 7 (TUT7) controls RNA stability by adding uridines to ... ...

Abstract	Different levels of regulatory mechanisms, including posttranscriptional regulation, are needed to elaborately regulate inflammatory responses to prevent harmful effects. Terminal uridyltransferase 7 (TUT7) controls RNA stability by adding uridines to its 3' ends, but its function in innate immune response remains obscure. Here we reveal that TLR4 activation induces TUT7, which in turn selectively regulates the production of a subset of cytokines, including Interleukin 6 (IL-6). TUT7 regulates IL-6 expression by controlling ribonuclease Regnase-1 mRNA (encoded by Zc3h12a gene) stability. Mechanistically, TLR4 activation causes TUT7 to bind directly to the stem-loop structure on Zc3h12a 3'-UTR, thereby promotes Zc3h12a uridylation and degradation. Zc3h12a from LPS-treated TUT7-sufficient macrophages possesses increased oligo-uridylated ends with shorter poly(A) tails, whereas oligo-uridylated Zc3h12a is significantly reduced in Tut7
MeSH term(s)	3' Untranslated Regions ; Animals ; Cytokines/genetics ; Cytokines/metabolism ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Humans ; Interleukin-6/genetics ; Interleukin-6/metabolism ; Lipopolysaccharides/pharmacology ; Macrophages/drug effects ; Macrophages/metabolism ; Mice ; Nucleotidyltransferases/metabolism ; RNA Stability ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Ribonucleases/genetics ; Ribonucleases/metabolism ; Toll-Like Receptor 4/metabolism ; Uridine Monophosphate/metabolism
Chemical Substances	3' Untranslated Regions ; Cytokines ; DNA-Binding Proteins ; Interleukin-6 ; Lipopolysaccharides ; RNA, Messenger ; Tlr4 protein, mouse ; Toll-Like Receptor 4 ; interleukin-6, mouse ; Uridine Monophosphate (E2OU15WN0N) ; Nucleotidyltransferases (EC 2.7.7.-) ; ZCCHC11 protein, mouse (EC 2.7.7.-) ; terminal uridylyl transferase 7, mouse (EC 2.7.7.-) ; Ribonucleases (EC 3.1.-) ; Zc3h12a protein, mouse (EC 3.1.-)
Language	English
Publishing date	2021-06-29
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-24177-7
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Article ; Online: Natural Modulators of Endosomal Toll-Like Receptor-Mediated Psoriatic Skin Inflammation.

Lai, Chao-Yang / Su, Yu-Wen / Lin, Kuo-I / Hsu, Li-Chung / Chuang, Tsung-Hsien

Journal of immunology research

2017 Volume 2017, Page(s) 7807313

Abstract: Psoriasis is a chronic inflammatory autoimmune disease that can be initiated by excessive activation of endosomal toll-like receptors (TLRs), particularly TLR7, TLR8, and TLR9. Therefore, inhibitors of endosomal TLR activation are being investigated for ... ...

Abstract	Psoriasis is a chronic inflammatory autoimmune disease that can be initiated by excessive activation of endosomal toll-like receptors (TLRs), particularly TLR7, TLR8, and TLR9. Therefore, inhibitors of endosomal TLR activation are being investigated for their ability to treat this disease. The currently approved biological drugs adalimumab, etanercept, infliximab, ustekinumab, ixekizumab, and secukizumab are antibodies against effector cytokines that participate in the initiation and development of psoriasis. Several immune modulatory oligonucleotides and small molecular weight compounds, including IMO-3100, IMO-8400, and CPG-52364, that block the interaction between endosomal TLRs and their ligands are under clinical investigation for their effectiveness in the treatment of psoriasis. In addition, several chemical compounds, including AS-2444697, PF-05387252, PF-05388169, PF-06650833, ML120B, and PHA-408, can inhibit TLR signaling. Although these compounds have demonstrated anti-inflammatory activity in animal models, their therapeutic potential for the treatment of psoriasis has not yet been tested. Recent studies demonstrated that natural compounds derived from plants, fungi, and bacteria, including mustard seed,
Language	English
Publishing date	2017
Publishing country	Egypt
Document type	Journal Article ; Review
ZDB-ID	2817541-4
ISSN	2314-7156 ; 2314-8861
ISSN (online)	2314-7156
ISSN	2314-8861
DOI	10.1155/2017/7807313
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Article: Toll-Like Receptor 21 of Chicken and Duck Recognize a Broad Array of Immunostimulatory CpG-oligodeoxynucleotide Sequences.

Chuang, Yu-Chen / Tseng, Jen-Chih / Yang, Jing-Xing / Liu, Yi-Ling / Yeh, Da-Wei / Lai, Chao-Yang / Yu, Guann-Yi / Hsu, Li-Chung / Huang, Chun-Ming / Chuang, Tsung-Hsien

Vaccines

2020 Volume 8, Issue 4

Abstract: CpG-oligodeoxynucleotides (CpG-ODNs) mimicking the function of microbial CpG-dideoxynucleotides containing DNA (CpG-DNA) are potent immune stimuli. The immunostimulatory activity and the species-specific activities of a CpG-ODN depend on its nucleotide ... ...

Abstract	CpG-oligodeoxynucleotides (CpG-ODNs) mimicking the function of microbial CpG-dideoxynucleotides containing DNA (CpG-DNA) are potent immune stimuli. The immunostimulatory activity and the species-specific activities of a CpG-ODN depend on its nucleotide sequence properties, including CpG-hexamer motif types, spacing between motifs, nucleotide sequence, and length. Toll-like receptor (TLR) 9 is the cellular receptor for CpG-ODNs in mammalian species, while TLR21 is the receptor in avian species. Mammalian cells lack TLR21, and avian cells lack TLR9; however, both TLRs are expressed in fish cells. While nucleotide sequence properties required for a CpG-ODN to strongly activate mammalian TLR9 and its species-specific activities to different mammalian TLR9s are better studied, CpG-ODN activation of TLR21 is not yet well investigated. Here we characterized chicken and duck TLR21s and investigated their activation by CpG-ODNs. Chicken and duck TLR21s contain 972 and 976 amino acid residues, respectively, and differ from TLR9s as they do not have an undefined region in their ectodomain. Cell-based TLR21 activation assays were established to investigate TLR21 activation by different CpG-ODNs. Unlike grouper TLR21, which was preferentially activated by CpG-ODN with a GTCGTT hexamer motif, chicken and duck TLR21s do not distinguish among different CpG-hexamer motifs. Additionally, these two poultry TLR21s were activated by CpG-ODNs with lengths ranging from 15 to 31 nucleotides and with different spacing between CpG-hexamer motifs. These suggested that compared to mammalian TLR9 and grouper TLR21, chicken and duck TLR21s have a broad CpG-ODN sequence recognition profile. Thus, they could also recognize a wide array of DNA-associated molecular patterns from microbes. Moreover, CpG-ODNs are being investigated as antimicrobial agents and as vaccine adjuvants for different species. This study revealed that there are more optimized CpG-ODNs that can be used in poultry farming as anti-infection agents compared to CpG-ODN choices available for other species.
Language	English
Publishing date	2020-11-02
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines8040639
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