Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus
The leucine-rich repeat (LRR) motif is evolutionarily conserved in many pattern recognition receptors. Compared to the reported LRR proteins with multiple functional domains, the role of LRR-only proteins merely containing LRR motifs remain largely unexplored. In this study, two LRR-only proteins, P...
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Frontiers Media S.A.
2022-07-01
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| Series: | Frontiers in Marine Science |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmars.2022.946182/full |
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| author | Ao Zhang Ao Zhang Yuan Liu Yuan Liu Yuan Liu Yuan Liu Na Guo Na Guo Shihao Li Shihao Li Shihao Li Shihao Li Fuhua Li Fuhua Li Fuhua Li Fuhua Li |
| author_facet | Ao Zhang Ao Zhang Yuan Liu Yuan Liu Yuan Liu Yuan Liu Na Guo Na Guo Shihao Li Shihao Li Shihao Li Shihao Li Fuhua Li Fuhua Li Fuhua Li Fuhua Li |
| author_sort | Ao Zhang |
| collection | DOAJ |
| description | The leucine-rich repeat (LRR) motif is evolutionarily conserved in many pattern recognition receptors. Compared to the reported LRR proteins with multiple functional domains, the role of LRR-only proteins merely containing LRR motifs remain largely unexplored. In this study, two LRR-only proteins, PtLRR1 and PtLRR2, were identified from the swimming crab Portunus trituberculatus. Five LRR motifs with a consensus sequence LxxLxxLxLxxNxL were found in their encoded peptides. Both PtLRR1 and PtLRR2 were dominantly expressed in the hepatopancreas and showed a time-dependent response post bacteria and virus stimulation. The recombinant PtLRR1 could bind to various PAMPs, including LPS, PGN, and GLU. PtLRR1 and PtLRR2 displayed different regulatory activities in inducing the expression of inflammation and proPO system-related genes. Knockdown of PtLRR2 led to the decreased expression of the tested cytokines and adapter, while PtLRR1 knockdown enhanced the expression of serine proteases, serine protease homologues, and proPO genes. In addition, knockdown of PtLRR1 or PtLRR2 reduced the clearance activity of Vibrio but upregulated the expression levels of AMPs and key genes of Toll, IMD, and JNK pathways. These results suggest that PtLRR1 and PtLRR2 could act as potential immune receptors and regulate antibacterial immunity in crab. |
| first_indexed | 2024-12-10T09:39:17Z |
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| id | doaj.art-f4e18a4b99e447239ec73c746399a3cc |
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| issn | 2296-7745 |
| language | English |
| last_indexed | 2024-12-10T09:39:17Z |
| publishDate | 2022-07-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Marine Science |
| spelling | doaj.art-f4e18a4b99e447239ec73c746399a3cc2022-12-22T01:54:05ZengFrontiers Media S.A.Frontiers in Marine Science2296-77452022-07-01910.3389/fmars.2022.946182946182Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatusAo Zhang0Ao Zhang1Yuan Liu2Yuan Liu3Yuan Liu4Yuan Liu5Na Guo6Na Guo7Shihao Li8Shihao Li9Shihao Li10Shihao Li11Fuhua Li12Fuhua Li13Fuhua Li14Fuhua Li15School of Marine Science and Engineering, Qingdao Agricultural University, Qingdao, ChinaChinese Academy of Sciences (CAS) and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaChinese Academy of Sciences (CAS) and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaLaboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaCenter for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, ChinaCollege of Marine Science University of Chinese Academy of Sciences, Beijing, ChinaSchool of Marine Science and Engineering, Qingdao Agricultural University, Qingdao, ChinaChinese Academy of Sciences (CAS) and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaChinese Academy of Sciences (CAS) and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaLaboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaCenter for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, ChinaCollege of Marine Science University of Chinese Academy of Sciences, Beijing, ChinaChinese Academy of Sciences (CAS) and Shandong Province Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaLaboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao, ChinaCenter for Ocean Mega-Science, Chinese Academy of Sciences, Qingdao, ChinaCollege of Marine Science University of Chinese Academy of Sciences, Beijing, ChinaThe leucine-rich repeat (LRR) motif is evolutionarily conserved in many pattern recognition receptors. Compared to the reported LRR proteins with multiple functional domains, the role of LRR-only proteins merely containing LRR motifs remain largely unexplored. In this study, two LRR-only proteins, PtLRR1 and PtLRR2, were identified from the swimming crab Portunus trituberculatus. Five LRR motifs with a consensus sequence LxxLxxLxLxxNxL were found in their encoded peptides. Both PtLRR1 and PtLRR2 were dominantly expressed in the hepatopancreas and showed a time-dependent response post bacteria and virus stimulation. The recombinant PtLRR1 could bind to various PAMPs, including LPS, PGN, and GLU. PtLRR1 and PtLRR2 displayed different regulatory activities in inducing the expression of inflammation and proPO system-related genes. Knockdown of PtLRR2 led to the decreased expression of the tested cytokines and adapter, while PtLRR1 knockdown enhanced the expression of serine proteases, serine protease homologues, and proPO genes. In addition, knockdown of PtLRR1 or PtLRR2 reduced the clearance activity of Vibrio but upregulated the expression levels of AMPs and key genes of Toll, IMD, and JNK pathways. These results suggest that PtLRR1 and PtLRR2 could act as potential immune receptors and regulate antibacterial immunity in crab.https://www.frontiersin.org/articles/10.3389/fmars.2022.946182/fullPortunus trituberculatusLeucine-rich repeatpattern recognition receptorRNA interferencesignaling pathway |
| spellingShingle | Ao Zhang Ao Zhang Yuan Liu Yuan Liu Yuan Liu Yuan Liu Na Guo Na Guo Shihao Li Shihao Li Shihao Li Shihao Li Fuhua Li Fuhua Li Fuhua Li Fuhua Li Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus Frontiers in Marine Science Portunus trituberculatus Leucine-rich repeat pattern recognition receptor RNA interference signaling pathway |
| title | Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus |
| title_full | Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus |
| title_fullStr | Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus |
| title_full_unstemmed | Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus |
| title_short | Two LRR-Only Proteins Involved in Antibacterial Defense and Prophenoloxidase System of Swimming Crab Portunus trituberculatus |
| title_sort | two lrr only proteins involved in antibacterial defense and prophenoloxidase system of swimming crab portunus trituberculatus |
| topic | Portunus trituberculatus Leucine-rich repeat pattern recognition receptor RNA interference signaling pathway |
| url | https://www.frontiersin.org/articles/10.3389/fmars.2022.946182/full |
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