In Silico Analysis of nsSNPs of Carp TLR22 Gene Affecting its Binding Ability with Poly I:C

Chakrapani, Vemulawada; Rasal, Kiran D.; Kumar, Sunil; Mohapatra, SD; Sundaray, Jitendra Kumar; Jayasankar, P.; Barman, Hirak Kumar

doi:10.1007/s12539-017-0247-2

Cited by 7 publications

(5 citation statements)

References 56 publications

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“…Selective mutations at LRR4–6 and LRR20–22 completely abolish poly(I:C) interactions, whereas LRR13–14 do not completely abolish poly(I:C) binding, but reduce the binding affinity [ 45 ]. Chakrapani et al, probed the binding interaction of poly(I:C) with a homology model structure of wild-type and mutant rohu TLR22 and observed complex instability in TLR22 mutant [ 128 ]. These findings highlights, docking simulation could be a powerful method to screen potential molecules for TLR activation.…”

Section: Structural Interactions Between Pamp and Prrmentioning

confidence: 99%

Structure of fish Toll-like receptors (TLR) and NOD-like receptors (NLR)

Sahoo

2020

International Journal of Biological Macromolecules

111

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Innate immunity driven by pattern recognition receptor (PRR) protects the host from invading pathogens. Aquatic animals like fish where the adaptive immunity is poorly developed majorly rely on their innate immunity modulated by PRRs like toll-like receptors (TLR) and NOD-like receptors (NLR). However, current development to improve the fish immunity via TLR/NLR signaling is affected by a poor understanding of its mechanistic and structural features. This review discusses the structure of fish TLRs/NLRs and its interaction with pathogen associated molecular patterns (PAMPs) and downstream signaling molecules. Over the past one decade, significant progress has been done in studying the structure of TLRs/NLRs in higher eukaryotes; however, structural studies on fish innate immune receptors are undermined. Several novel TLR genes are identified in fish that are absent in higher eukaryotes, but the function is still poorly understood. Unlike the fundamental progress achieved in developing antagonist/agonist to modulate human innate immunity, analogous studies in fish are nearly lacking due to structural inadequacy. This underlies the importance of exploring the structural and mechanistic details of fish TLRs/NLRs at an atomic and molecular level. This review outlined the mechanistic and structural basis of fish TLR and NLR activation.

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Section: Structural Interactions Between Pamp and Prrmentioning

confidence: 99%

Structure of fish Toll-like receptors (TLR) and NOD-like receptors (NLR)

Sahoo

2020

International Journal of Biological Macromolecules

111

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“…Is it structurally complementary or affected by charge? Previous research predicted that mutations at p.L159F and p.L529P in the LRR region affect the binding affinity significantly (16). Although there is no direct evidence, it serves as a guide for later research.…”

Section: Discussionmentioning

confidence: 99%

“…It has been proved that TLR22 responded to poly(I:C) and involved in antiviral immunity in many species, including orange-spotted grouper (Epinephelus coioides) (14), large yellow croaker (Pseudosciaena crocea) (15). In addition, Chakrapani et al predicted that the mutation of LRR in TLR22 affects its binding ability with poly(I:C) in Labeo rohita (16). These results support that TLR22 has a conservative function in responding to dsRNA among different species.…”

Section: Introductionmentioning

confidence: 99%

Thoroughly Remold the Localization and Signaling Pathway of TLR22

Liao

Rao

et al. 2020

Front. Immunol.

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TLR22 exists in nearly all the poikilothermic vertebrates and plays a central role in the initiation of innate immunity and activation of adaptive immunity. TLR22 signaling pathway has been characterized in detail in fugu (Takifugu rubripes). Here, we thoroughly remold the localization and signaling pathways of TLR22. We characterized TLR22a and TLR22b in grass carp (Ctenopharyngodon idella), designated as CiTLR22a and CiTLR22b, and explored the ligand(s), adaptor(s), and signaling pathway(s). Results show that both CiTLR22a and CiTLR22b localize to lysosome, acidic compartment. Correspondingly, CiTLR22a and CiTLR22b directly bind and respond to dsRNA analog poly(I:C) at pH 5, but not at pH 7.4, the physiological pH. Moreover, CiTLR22a and CiTLR22b exhibit antagonistic function in signal transmission, wherein CiTLR22a facilitates the protein and phosphorylation levels of IRF7 and enhances the promoter activities of major IFNs and NF-κBs, while CiTLR22b downregulates IRF7 phosphorylation and IRF3 protein level and suppresses the IFN and NF-κB pathways. Further investigations revealed that CiTLR22a restrains grass carp reovirus (GCRV) replication and protects cells from GCRV infection, whereas CiTLR22b plays a negative role in response to GCRV infection. This is the first time to systematically clarify the signaling pathways of two isotype TLR22s; especially, subcellular localization and adaptor are different from previous TLR22 report, which results from technical limitations. The results will serve the antiviral immune mechanisms in poikilothermic vertebrates and evolutionary immunology.

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“…Nhiều nghiên cứu chỉ ra rằng TLR22 phản ứng với một chất tổng hợp mô phỏng dsRNA là olyinosinic acid: olycytidylic acid (poly(I:C)), điều này xuất hiện ở cá đù vàng lớn, cá trôi Ấn Độ, cá nóc, cá trăm cỏ hay cá ngựa vằn và cá tuyết 19,22,25,26,30,36,40 . Việc gây đột biến trong vùng LRR của TLR22 ở cá trôi Ấn Độ đã ảnh hưởng đến khả năng liên kết với poly(I:C) 41 . Các kết quả trên cho thấy TLR22 có chức năng nhân diện và tương tác với dsDNA và chức năng này được bảo tồn giữa các loài cá khác nhau.…”

Section: Chức Năng Tlr22unclassified