Journal
FISH & SHELLFISH IMMUNOLOGY
Volume 114, Issue -, Pages 161-170Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fsi.2021.04.022
Keywords
Fibrinogen-like protein; Innate immunity; Pattern recognition receptors; Vibrio splendidus; Crassostrea gigas
Funding
- National Science Foundation of China [31972817, 31802336, U1706204]
- National Key RD Program [2018YFD0900504]
- earmarked fund from Modern Agroindustry Technology Research System [CARS-49]
- Fund for Outstanding Talents and Innovative Team of Agricultural Scientific Research, Liaoning Climbing Scholar
- Young Science and Technology Talents Seedling Program of Educational Department of Liaoning Province [QL201903]
- Research Foundation for Talented Scholars in Dalian Ocean University
- Initiated Program of Introducing Talents in Dalian Ocean University [HDYJ201825]
- [XLYC1902012]
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CgFREP1, identified in oysters, serves as a pattern recognition receptor to recognize and agglutinate various bacteria, as well as mediate haemocytes phagocytosis towards Vibrio splendidus.
The family of fibrinogen-related proteins (FREPs) is a group of proteins with fibrinogen-like (FBG) domains, which play important roles as pattern recognition receptors (PRRs) in the innate immune responses. In the present study, a fibrinogen-like protein was identified from the oyster Crassostrea gigas (defined as CgFREP1). The open reading frame of CgFREP1 was of 966 bp that encoded a predicted polypeptide of 321 amino acids comprising a signal peptide and a fibrinogen-like domain. The mRNA expression of CgFREP1 was detected in all the examined tissues. The recombinant CgFREP1 (rCgFREP1) displayed binding activities to lipopolysaccharide (LPS), mannose (MAN), as well as Gram-positive bacteria (Micrococcus luteus and Staphylococcus aureus) and Gram-negative bacteria (Vibrio splendidus and Escherichia coli). The rCgFREP1 displayed the agglutinating activity towards M. luteus, V. splendidus and E. coli in the presence of Ca2+. rCgFREP1 was able to enhance the phagocytic activity of haemocytes towards V. splendidus, and exhibited binding activity to the CUB domain of CgMASPL-1. These results suggest that CgFREP1 not only serves as a PRR to recognize and agglutinate different bacteria but also mediates the haemocytes phagocytosis towards V. splendidus.
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