A C1qDC Protein (HcC1qDC6) with Three Tandem C1q Domains Is Involved in Immune Response of Triangle-Shell Pearl Mussel (Hyriopsis cumingii)

Huang, Ying; Wu, Lei; Jin, Min; Hui, Kai-Min; Ren, Qian

doi:10.3389/fphys.2017.00521

Cited by 19 publications

(9 citation statements)

References 41 publications

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“…The cumulative mortality of MjFREP2-silenced shrimp was rather higher than that of the control group [27]. In Hyriopsis cumingii, knockdown of HcC1qDC6 inhibited the expression of tumor necrosis factor and whey acidic protein [28,29]. In the present study, reduced expression of RpSabl transcirpts down-regulated the expression of several immune effectors in the hemolymph, indicating that clam mortality was attributable to the down-regulation of these immune effectors.…”

Section: Discussionmentioning

confidence: 43%

A sialic acid-binding lectin with bactericidal and opsonic activities from Ruditapes philippinarum

Zhang

et al. 2019

Fish & Shellfish Immunology

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In the present study, a sialic acid-binding lectin was cloned and characterized from Manila clam Ruditapes philippinarum (designed as RpSabl). The open reading frame of RpSabl encoded a polypeptide of 162 amino acids with a calculated molecular mass of 17.7 kDa. Analysis of the conserved domain suggested that RpSabl was a new member of the sialic acid-binding lectins family. In non-stimulated clams, RpSabl transcripts were constitutively expressed in all five tested tissues, especially in hepatopancreas. After Vibrio anguillarum challenge, the expression of RpSabl mRNA in hepatopancreas was significantly up-regulated at 3 h (3.8-fold, P < 0.05), 6 h (4.9-fold, P < 0.05), 12 h (12.3-fold, P < 0.01) and 24 h (9.7-fold, P < 0.01), while RpSabl transcripts in hemocytes was only significantly up-regulated at 6 h (8.5-Fold, P < 0.01). RNAi-mediated knockdown of RpSabl transcripts affected the survival rates of Manila clam against V. anguillarum, perhaps mainly due to the inhibited expression of antibacterial effectors (e.g. lysozyme and defensin). Moreover, recombinant protein of RpSabl (rRpSabl) possessed binding activities towards lipopolysaccharides (LPS), peptidoglycan (PGN) and glucan in vitro. Coinciding with the Pathogen-associated molecular patterns (PAMPs) binding assay, rRpSabl displayed broad bacterial-agglutination properties towards Vibrio harveyi, Vibrio splendidus, V. anguillarum, Enterobacter cloacae and Aeromonas hydrophila. Meanwhile, the phagocytosis and encapsulation ability of hemocytes could be significantly enhanced by rRpSabl incubation. All these results showed that RpSabl could function as a versatile molecule involved in the innate immune responses of R. philippinarum.

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Section: Discussionmentioning

confidence: 43%

A sialic acid-binding lectin with bactericidal and opsonic activities from Ruditapes philippinarum

Zhang

et al. 2019

Fish & Shellfish Immunology

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“…However, the expression level in hemocytes was relatively low. We speculate that, similar to HcC1qDC6 20 , PmC1qDC-1 expression in hemocytes may be induced under stress. As such, the challenge experiment of LPS and poly I:C was performed to further understand the immune-related functions of PmC1qDC-1 in pearl oysters.…”

Section: Discussionmentioning

confidence: 88%

“…C1qDC proteins, which are pattern recognition molecules, rely on their gC1q domain to recognize a variety of self and non-self ligands, including a vast range of PAMPs of bacteria, yeast, viruses, and parasites 20 , 45 . The shell notching experiment indicates that PmC1qDC-1 participates in the immune process.…”

Section: Discussionmentioning

confidence: 99%

“…MgC1q gene is involved in host defense in Mytilus galloprovincialis 19 . HcC1qDC6 is involved in innate immunity by directly binding to peptidoglycan (PGN) and LPS in Hyriopsis cumingii 20 . In Crassostrea gigas , CgC1qDC-6 mediates hemocyte phagocytosis and migration and can bind to various pathogen-associated molecular patterns (PAMPs), including LPS, PGN, mannose and poly I:C, and microorganisms 21 .…”

Section: Introductionmentioning

confidence: 99%

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Novel globular C1q domain-containing protein (PmC1qDC-1) participates in shell formation and responses to pathogen-associated molecular patterns stimulation in Pinctada fucata martensii

Xiong

Zheng

et al. 2021

Sci Rep

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The C1q protein, which contains the globular C1q (gC1q) domain, is involved in the innate immune response, and is found abundantly in the shell, and it participates in the shell formation. In this study, a novel gC1q domain-containing gene was identified from Pinctada fucata martensii (P. f. martensii) and designated as PmC1qDC-1. The full-length sequence of PmC1qDC-1 was 902 bp with a 534 bp open reading frame (ORF), encoding a polypeptide of 177 amino acids. Quantitative real-time PCR (qRT-PCR) result showed that PmC1qDC-1 was widely expressed in all tested tissues, including shell formation-associated tissue and immune-related tissue. PmC1qDC-1 expression was significantly high in the blastula and gastrula and especially among the juvenile stage, which is the most important stage of dissoconch shell formation. PmC1qDC-1 expression was located in the outer epithelial cells of mantle pallial and mantle edge and irregular crystal tablets were observed in the nacre upon knockdown of PmC1qDC-1 expression at mantle pallial. Moreover, the recombined protein PmC1qDC-1 increased the rate of calcium carbonate precipitation. Besides, PmC1qDC-1 expression was significantly up-regulated in the mantle pallial at 6 h and was significantly up-regulated in the mantle edge at 12 h and 24 h after shell notching. The expression level of PmC1qDC-1 in mantle edge was significantly up-regulated at 48 h after LPS stimulation and was significantly up-regulated at 12 h, 24 h and 48 h after poly I:C stimulation. Moreover, PmC1qDC-1 expression was significantly up-regulated in hemocytes at 6 h after lipopolysaccharide (LPS) and poly I:C challenge. These findings suggest that PmC1qDC-1 plays a crucial role both in the shell formation and the innate immune response in pearl oysters, providing new clues for understanding the shell formation and defense mechanism in mollusk.

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“…C1qDC proteins have been found to be immune factors in many cases. Various pathogens and their components induce an increase in C1qDC proteins expression, as well as C1qDC proteins demonstrating the ability to bind PDG, LPS, poly I:C, mannan, β-1,3-glucan, yeast glucan and live bacteria, generally indicating their role as PRRs [9][10][11][12][13][18][19][20][31][32][33][34][35][36][37][38]. Agglutinating activity of MkC1qDC was observed against Grampositive and Gram-negative bacteria, but with slightly more pronounced selectivity for certain strains, such as Pseudoalteromonas sp.…”

Section: Discussionmentioning

confidence: 99%

A Novel C1q Domain-Containing Protein Isolated from the Mollusk Modiolus kurilensis Recognizing Glycans Enriched with Acidic Galactans and Mannans

et al. 2021

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C1q domain-containing (C1qDC) proteins are a group of biopolymers involved in immune response as pattern recognition receptors (PRRs) in a lectin-like manner. A new protein MkC1qDC from the hemolymph plasma of Modiolus kurilensis bivalve mollusk widespread in the Northwest Pacific was purified. The isolation procedure included ammonium sulfate precipitation followed by affinity chromatography on pectin-Sepharose. The full-length MkC1qDC sequence was assembled using de novo mass-spectrometry peptide sequencing complemented with N-terminal Edman’s degradation, and included 176 amino acid residues with molecular mass of 19 kDa displaying high homology to bivalve C1qDC proteins. MkC1qDC demonstrated antibacterial properties against Gram-negative and Gram-positive strains. MkC1qDC binds to a number of saccharides in Ca2+-dependent manner which characterized by structural meta-similarity in acidic group enrichment of galactose and mannose derivatives incorporated in diversified molecular species of glycans. Alginate, κ-carrageenan, fucoidan, and pectin were found to be highly effective inhibitors of MkC1qDC activity. Yeast mannan, lipopolysaccharide (LPS), peptidoglycan (PGN) and mucin showed an inhibitory effect at concentrations three orders of magnitude greater than for the most effective saccharides. MkC1qDC localized to the mussel hemal system and interstitial compartment. Intriguingly, MkC1qDC was found to suppress proliferation of human adenocarcinoma HeLa cells in a dose-dependent manner, indicating to the biomedical potential of MkC1qDC protein.

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A C1qDC Protein (HcC1qDC6) with Three Tandem C1q Domains Is Involved in Immune Response of Triangle-Shell Pearl Mussel (Hyriopsis cumingii)

Cited by 19 publications

References 41 publications

A sialic acid-binding lectin with bactericidal and opsonic activities from Ruditapes philippinarum

A sialic acid-binding lectin with bactericidal and opsonic activities from Ruditapes philippinarum

Novel globular C1q domain-containing protein (PmC1qDC-1) participates in shell formation and responses to pathogen-associated molecular patterns stimulation in Pinctada fucata martensii

A Novel C1q Domain-Containing Protein Isolated from the Mollusk Modiolus kurilensis Recognizing Glycans Enriched with Acidic Galactans and Mannans

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