Journal
FRONTIERS IN IMMUNOLOGY
Volume 13, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fimmu.2022.869845
Keywords
scallop; innate immunity; IKK; MyD88; IRF; signaling pathway
Categories
Funding
- Agricultural Variety Improvement Project of Shandong Province [2019LZGC020]
- National Key R&D Program of China [2018YFD0901400]
- National Natural Science Foundation of China [31802328, 41876193, 41906088, 42076088]
- Special Funds for Taishan Scholars Project of Shandong Province, China [tsqn201812094]
- Shandong Provincial Natural Science Foundation, China [ZR2019MC002]
- Modern Agricultural Industry Technology System of Shandong Province, China [SDAIT-14-03]
- Plan of Excellent Youth Innovation Team of Colleges and Universities in Shandong Province, China [2019KJF004]
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IKK proteins play important roles in the innate immune system of animals. In this study, the CfIKK1 gene was cloned from the Zhikong scallop and its function and signaling were investigated. CfIKK1 was found to respond to pathogen associated molecular patterns (PAMPs) challenge and interact with MyD88 protein, forming dimers or oligomers. RNAi experiments confirmed the regulatory relationship between IKK1 and IRF genes in scallops.
IKK proteins are key signaling molecules in the innate immune system of animals, and act downstream of pattern recognition receptors. However, research on IKKs in invertebrates, especially marine mollusks, remains scarce. In this study, we cloned CfIKK1 gene from the Zhikong scallop (Chlamys farreri) and studied its function and the signaling it mediates. The open reading frame of CfIKK1 was 2190 bp and encoded 729 amino acids. Phylogenetic analysis showed that CfIKK1 belonged to the invertebrate IKK alpha/IKK beta family. Quantitative real-time PCR analysis revealed the ubiquitous expression of CfIKK1 mRNA in all scallop tissues and challenge with lipopolysaccharide, peptidoglycan, or poly(I:C) significantly upregulated the expression of CfIKK1. Co-immunoprecipitation assays confirmed the interaction of CfIKK1 with scallop MyD88 (Myeloid differentiation actor 88, the key adaptor of the TLR signaling pathway) via its N-terminal kinase domain. Additionally, CfIKK1 protein could form homodimers and even oligomers, with N-terminal kinase domain and C-terminal scaffold dimerization domain playing key roles in this process. Finally, the results of RNAi experiments showed that when the scallop IKK1 gene was suppressed, the expression of IRF genes also decreased significantly. In conclusion, CfIKK1 could respond to PAMPs challenge and interact with MyD88 protein of scallop TLR signaling, with the formation of CfIKK1 dimers or oligomers. At the same time, the results of RNAi experiments revealed the close regulatory relationship between IKK1 and IRF genes of scallop. Therefore, as a key signal transduction molecule and immune activity regulator, CfIKK1 plays important roles in the innate immune system of scallops.
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