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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Bibliographic Details
Main Authors: Meijia Li, Leilei Wang, Lingling Wang, Weilin Wang, Chuanyan Yang, Linsheng Song
Format: Article
Language:English
Published: Elsevier 2025-06-01
Series:Comparative Immunology Reports
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Online Access:http://www.sciencedirect.com/science/article/pii/S2950311624000570
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Summary: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.
ISSN:2950-3116