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A novel globular C1q domain containing protein (C1qDC-7) from Crassostrea gigas acts as pattern recognition receptor with broad recognition spectrum
- Zong, Yanan, Liu, Zhaoqun, Wu, Zhaojun, Han, Zirong, Wang, Lingling, Song, Linsheng
- Fish & shellfish immunology 2019 v.84 pp. 920-926
- Aeromonas hydrophila, Crassostrea gigas, Crassostrea virginica, Escherichia coli, Gram-negative bacteria, Gram-positive bacteria, Komagataella pastoris, Micrococcus luteus, Mizuhopecten yessoensis, Mytilus galloprovincialis, Staphylococcus aureus, Vibrio alginolyticus, Vibrio anguillarum, Vibrio splendidus, Yarrowia lipolytica, amino acids, binding capacity, fish, fungi, gills, hemocytes, hepatopancreas, immunology, ligands, lipopolysaccharides, messenger RNA, muscles, open reading frames, palps, pathogen-associated molecular patterns, peptidoglycans, phylogeny, polypeptides, receptors, recombinant proteins, shellfish, tissues
- The globular C1q domain containing (C1qDC) proteins are a family of versatile pattern recognition receptors (PRRs) to bind various ligands by their globular C1q (gC1q) domain. In the present study, a novel globular C1qDC (CgC1qDC-7) was characterized from Pacific oyster Crassostrea gigas. The open reading frame of CgC1qDC-7 was of 555 bp, encoding a polypeptide of 185 amino acids. Phylogenetic analysis indicated that CgC1qDC-7 shared high homology with C1qDCs from Crassostrea virginica, Mytilus galloprovincialis, and Mizuhopecten yessoensis. The mRNA transcripts of CgC1qDC-7 were widely expressed in all the tested tissues including mantle, gonad, gills, adductor muscle, hemocytes, hepatopancreas and labial palps, with the highest expression level in hemocytes and gills. The recombinant protein of CgC1qDC-7 (rCgC1qDC-7) exhibited binding activity towards Gram-negative bacteria (Vibrio splendidus, V. anguillarum, Escherichia coli, V. alginolyticus, and Aeromonas hydrophila), Gram-positive bacteria (Micrococcus luteus and Staphylococcus aureus) and fungi (Pichia pastoris and Yarrowia lipolytica), and displayed strongest binding affinity towards Gram-negative bacteria V. splendidus and V. anguillarum. It also exhibited affinity to vital pathogen-associated molecular patterns (PAMPs), such as lipopolysaccharide (LPS), peptidoglycan (PGN), mannan (MAN) and Poly (I:C) with high affinity towards LPS and PGN, and low affinity to MAN and Poly (I:C). These results collectively indicated that CgC1qDC-7 was a novel PRR in C. gigas with high binding affinity towards LPS and PGN as well as Gram-negative bacteria.