Four C1q domain-containing proteins involved in the innate immune response in Hyriopsis cumingii

Zhao, Lingling; Jin, Min; Li, Xin-Cang; Ren, Qian; Lan, Jiang-Feng

doi:10.1016/j.fsi.2016.06.003

Cited by 15 publications

(13 citation statements)

References 31 publications

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“…The HcC1qDC6 mRNA is constitutively expressed in the mantles, hepatopancreas, hemocytes, and gills, which is similar to that found in HcC1qDC1 to HcC1qDC5 from H. cumingii (Huang et al, 2016; Zhao et al, 2016), AiC1qDC-1 and AiC1qDC-2 from A. irradians (Kong et al, 2010; Wang et al, 2012a), CfC1qDC from C. farreri (Jiang et al, 2015), and L-C1qDC-1 from Lethenteron camtschaticum (Pei et al, 2016). The HcC1qDC6 transcript is highly expressed in the mantle and mantle tissue plays a crucial role in pathogen prevention and clearance (Wang et al, 2013).…”

Section: Discussionsupporting

confidence: 62%

“…Three gC1q domains strongly bind to Gram-negative and Gram-positive bacteria. In addition, HcC1qDC proteins also exhibited a good binding ability (Huang et al, 2016; Zhao et al, 2016). …”

Section: Discussionmentioning

confidence: 99%

“…The expansion of C1qDC and other immune-related genes allows the mussels to adapt to different environments. Previous studies reveal that five C1qDC genes are involved in the innate immunity of H. cumingii (Huang et al, 2016; Zhao et al, 2016). In the present study, a C1qDC gene HcC1qDC6 was detected from H. cumingii .…”

Section: Introductionmentioning

confidence: 99%

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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)

Huang

Jin³

et al. 2017

Front. Physiol.

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C1q-domain-containing (C1qDC) proteins are a family of proteins with a globular C1q (gC1q) domain and participate in several immune responses. In this study, a C1qDC gene was identified from the triangle-shell pearl mussel Hyriopsis cumingii (designated as HcC1qDC6). This gene has a full-length cDNA of 1782 bp and an open reading frame of 1,335 bp that encodes a 444-amino acid polypeptide containing three gC1q domains. HcC1qDC6 contains at least five exons and four introns. The mRNA transcripts of HcC1qDC6 were found to have the highest expression levels in the mantle tissue. The expression levels in the mantle and hepatopancreas were significantly upregulated by Staphylococcus aureus and Vibrio parahaemolyticus challenges. Moreover, knockdown of HcC1qDC6 inhibits the expression of two immune-related genes (tumor necrosis factor and whey acidic protein). The recombinant proteins of C1q1, C1q2, and C1q3 all exhibit a binding activity against seven bacterial species and directly bind to peptidoglycan and lipopolysaccharide. The results indicate that HcC1qDC6 is involved in the innate immunity of H. cumingii.

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Section: Discussionsupporting

confidence: 62%

“…Three gC1q domains strongly bind to Gram-negative and Gram-positive bacteria. In addition, HcC1qDC proteins also exhibited a good binding ability (Huang et al, 2016; Zhao et al, 2016). …”

Section: Discussionmentioning

confidence: 99%

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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)

Huang

Jin³

et al. 2017

Front. Physiol.

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“…Experimental challenges have further demonstrated that many bivalve C1qDC genes are induced by infection with various Gram-positive and Gram-negative bacteria, as well as by fungi (Kong et al 2010;Gestal et al 2010;Li et al 2011a;Gerdol et al 2011;Jiang et al 2015), but also by direct stimulation with LPS, PGN, β-glucan, and polyI:C (Wang et al 2012a(Wang et al , b, 2015aYang et al 2012), altogether reinforcing their role as PRRs. The indications collected from gene expression studies were later confirmed by the binding properties of C1qDC recombinant proteins toward LPS, PGN, polyI:C, mannan, β-1,3-glucan, and yeast glucan (Wang et al 2012a(Wang et al , 2015aJiang et al 2015) as well as toward live bacteria (Wang et al 2015a;Zhao et al 2016a;Huang et al 2016).…”

Section: Functional Studies Are Progressively Revealing the Immune Fu...mentioning

confidence: 82%

Immunity in Molluscs: Recognition and Effector Mechanisms, with a Focus on Bivalvia

Gerdol

Gomez‐Chiarri

Castillo

et al. 2018

Advances in Comparative Immunology

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The study of molluscan immune systems, and in particular those of bivalve molluscs (clams, oysters, scallops, mussels, etc.) has experienced great growth in recent decades, mainly due to the needs of a rapidly growing aquaculture industry to manage the impacts of disease and the application of -omic tools to this diverse group of invertebrate organisms. Several unique aspects of molluscan immune systems highlighted in this chapter include the importance of feeding behavior and mucosal immunity, the discovery of unique levels of diversity in immune genes, and experimental indication of transgenerational immune priming. The development of comparative functional studies using natural and selectively bred disease-resistant strains, together with the potential but yet to be fully developed application of gene-editing technologies, should provide exciting insights into the functional relevance of immune gene family expansion and molecular diversification in bivalves. Other areas of bivalve immunity that deserve further study include elucidation of the process of hematopoiesis, the molecular characterization of hemocyte subpopulations, and the genetic and molecular mechanisms underlying immune priming. While the most important aspects of the immune system of the largest group of molluscs, gastropods (e.g., snails and slugs), are discussed in detail in Chap. 12, we also briefly outline the most distinctive features of the immune system of another fascinating group of marine molluscs, cephalopods, which include invertebrate animals with extraordinary morphological and behavioral complexity.

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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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Four C1q domain-containing proteins involved in the innate immune response in Hyriopsis cumingii

Cited by 15 publications

References 31 publications

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

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

Immunity in Molluscs: Recognition and Effector Mechanisms, with a Focus on Bivalvia

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

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