A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule
Fibrinogen-related proteins (FREPs) have been reported to exhibit extensive expansion with remarkable structural diversity in invertebrate genomes, particularly in mollusks, which execute multifaceted functions ranging from non-self recognition to clot formation. In the present study, a FREP was ide...
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Elsevier
2025-06-01
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| Series: | Comparative Immunology Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2950311624000570 |
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| author | Meijia Li Leilei Wang Lingling Wang Weilin Wang Chuanyan Yang Linsheng Song |
| author_facet | Meijia Li Leilei Wang Lingling Wang Weilin Wang Chuanyan Yang Linsheng Song |
| author_sort | Meijia Li |
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| description | Fibrinogen-related proteins (FREPs) have been reported to exhibit extensive expansion with remarkable structural diversity in invertebrate genomes, particularly in mollusks, which execute multifaceted functions ranging from non-self recognition to clot formation. In the present study, a FREP was identified in Zhikong scallop, Chlamys farreri (named as CfFREP), which contained a signal peptide, a conserved fibrinogen-related domain (FBG), and two additional coiled-coil regions. CfFREP clustered closely with the FREP from Argopecten irradians in the phylogenetic tree. The endogenous CfFREP protein was predominantly localized in immune-related tissues, including the hepatopancreas, gill, kidney, and haemocytes. The mRNA expression of CfFREP in haemocytes was significantly upregulated at 12 h post stimulation with lipopolysaccharides (LPS) and peptidoglycan (PGN), exhibiting a 10.8-fold (p < 0.05) and 6.7-fold (p < 0.01) increase, respectively, compared to the PBS control group. However, no significant change was observed in response to β-glucan (GLU) (p > 0.05). The recombinant protein (rCfFREP) displayed varied binding activities towards four different pathogen-associated molecular patterns (PAMPs) in a dose-dependent manner, with much higher affinity towards LPS and Poly I:C compared to PGN and β-glucan. These findings collectively suggested that CfFREP functioned as a canonical immune recognition molecule in scallop, which offers fresh perspectives on the functions of mollusk FREPs. |
| format | Article |
| id | doaj-art-f3eb2dcb75e941bd8e95606adaebfbe5 |
| institution | Kabale University |
| issn | 2950-3116 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
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| series | Comparative Immunology Reports |
| spelling | doaj-art-f3eb2dcb75e941bd8e95606adaebfbe52024-12-28T05:23:18ZengElsevierComparative Immunology Reports2950-31162025-06-018200190A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition moleculeMeijia Li0Leilei Wang1Lingling Wang2Weilin Wang3Chuanyan Yang4Linsheng Song5Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian 116023, China; Liaoning Key Laboratory of Marine Animal Immunology and Disease Control, Dalian Ocean University, Dalian 116023, China; Dalian Key Laboratory of Aquatic Animal Diseases Prevention and Control, Dalian Ocean University, Dalian 116023, ChinaKey Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, ChinaLiaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian 116023, China; Liaoning Key Laboratory of Marine Animal Immunology and Disease Control, Dalian Ocean University, Dalian 116023, China; Dalian Key Laboratory of Aquatic Animal Diseases Prevention and Control, Dalian Ocean University, Dalian 116023, China; Corresponding authors at:Dalian Ocean University, Dalian 116023, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian 116023, China; Liaoning Key Laboratory of Marine Animal Immunology and Disease Control, Dalian Ocean University, Dalian 116023, China; Dalian Key Laboratory of Aquatic Animal Diseases Prevention and Control, Dalian Ocean University, Dalian 116023, ChinaLiaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian 116023, China; Liaoning Key Laboratory of Marine Animal Immunology and Disease Control, Dalian Ocean University, Dalian 116023, China; Dalian Key Laboratory of Aquatic Animal Diseases Prevention and Control, Dalian Ocean University, Dalian 116023, China; Corresponding authors at:Dalian Ocean University, Dalian 116023, China.Liaoning Key Laboratory of Marine Animal Immunology, Dalian Ocean University, Dalian 116023, China; Liaoning Key Laboratory of Marine Animal Immunology and Disease Control, Dalian Ocean University, Dalian 116023, China; Dalian Key Laboratory of Aquatic Animal Diseases Prevention and Control, Dalian Ocean University, Dalian 116023, ChinaFibrinogen-related proteins (FREPs) have been reported to exhibit extensive expansion with remarkable structural diversity in invertebrate genomes, particularly in mollusks, which execute multifaceted functions ranging from non-self recognition to clot formation. In the present study, a FREP was identified in Zhikong scallop, Chlamys farreri (named as CfFREP), which contained a signal peptide, a conserved fibrinogen-related domain (FBG), and two additional coiled-coil regions. CfFREP clustered closely with the FREP from Argopecten irradians in the phylogenetic tree. The endogenous CfFREP protein was predominantly localized in immune-related tissues, including the hepatopancreas, gill, kidney, and haemocytes. The mRNA expression of CfFREP in haemocytes was significantly upregulated at 12 h post stimulation with lipopolysaccharides (LPS) and peptidoglycan (PGN), exhibiting a 10.8-fold (p < 0.05) and 6.7-fold (p < 0.01) increase, respectively, compared to the PBS control group. However, no significant change was observed in response to β-glucan (GLU) (p > 0.05). The recombinant protein (rCfFREP) displayed varied binding activities towards four different pathogen-associated molecular patterns (PAMPs) in a dose-dependent manner, with much higher affinity towards LPS and Poly I:C compared to PGN and β-glucan. These findings collectively suggested that CfFREP functioned as a canonical immune recognition molecule in scallop, which offers fresh perspectives on the functions of mollusk FREPs.http://www.sciencedirect.com/science/article/pii/S2950311624000570Scallop Chlamys farreriFibrinogen-related proteinCoiled-coil regionImmune responseImmune recognition |
| spellingShingle | Meijia Li Leilei Wang Lingling Wang Weilin Wang Chuanyan Yang Linsheng Song A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule Comparative Immunology Reports Scallop Chlamys farreri Fibrinogen-related protein Coiled-coil region Immune response Immune recognition |
| title | A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule |
| title_full | A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule |
| title_fullStr | A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule |
| title_full_unstemmed | A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule |
| title_short | A novel fibrinogen-related protein with two coiled-coil regions from Chlamys farreri functions as immune recognition molecule |
| title_sort | novel fibrinogen related protein with two coiled coil regions from chlamys farreri functions as immune recognition molecule |
| topic | Scallop Chlamys farreri Fibrinogen-related protein Coiled-coil region Immune response Immune recognition |
| url | http://www.sciencedirect.com/science/article/pii/S2950311624000570 |
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