A C1q Domain Containing Protein from Scallop Chlamys Farreri Serving As Pattern Recognition Receptor with Heat-aggregated IgG Binding Activity

Overview

Journal PLoS One

Specialties General Medicine
Science

Date 2012 Aug 21

PMID 22905248

Citations 14

Authors

Leilei Wang

Lingling Wang

Huan Zhang

Zhi Zhou

Vinu S Siva

Linsheng Song

Affiliations

Soon will be listed here.

Abstract

Background: The C1q domain containing (C1qDC) proteins refer to a family of all proteins that contain the globular C1q (gC1q) domain, and participate in a series of immune responses depending on their gC1q domains to bind a variety of self and non-self binding ligands.

Methodology: In the present study, the mRNA expression patterns, localization, and activities of a C1qDC protein from scallop Chlamys farreri (CfC1qDC) were investigated to understand its possible functions in innate immunity. The relative expression levels of CfC1qDC mRNA in hemocytes were all significantly up-regulated after four typical PAMPs (LPS, PGN, β-glucan and polyI:C) stimulation. During the embryonic development of scallop, the mRNA transcripts of CfC1qDC were detected in all the stages, and the expression level was up-regulated from D-hinged larva and reached the highest at eye-spot larva. The endogenous CfC1qDC was dominantly located in the hepatopancreas, gill, kidney and gonad of adult scallop through immunofluorescence. The recombinant protein of CfC1qDC (rCfC1qDC) could not only bind various PAMPs, such as LPS, PGN, β-glucan as well as polyI:C, but also enhance the phagocytic activity of scallop hemocytes towards Escherichia coli. Meanwhile, rCfC1qDC could interact with human heat-aggregated IgG, and this interaction could be inhibited by LPS.

Conclusions: All these results indicated that CfC1qDC in C. farreri not only served as a PRR involved in the PAMPs recognition, but also an opsonin participating in the clearance of invaders in innate immunity. Moreover, the ability of CfC1qDC to interact with immunoglobulins provided a clue to understand the evolution of classical pathway in complement system.

Citing Articles

Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential.

Grinchenko A, Buriak I, Kumeiko V Mar Drugs. 2023; 21(11).

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Specification of hemocyte subpopulations based on immune-related activities and the production of the agglutinin MkC1qDC in the bivalve .

Sokolnikova Y, Mokrina M, Magarlamov T, Grinchenko A, Kumeiko V Heliyon. 2023; 9(4):e15577.

PMID: 37151667 PMC: 10161718. DOI: 10.1016/j.heliyon.2023.e15577.

A tick C1q protein alters infectivity of the Lyme disease agent by modulating interferon γ.

Tang X, Arora G, Matias J, Hart T, Cui Y, Fikrig E Cell Rep. 2022; 41(8):111673.

PMID: 36417869 PMC: 9909562. DOI: 10.1016/j.celrep.2022.111673.

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

Grinchenko A, von Kriegsheim A, Shved N, Egorova A, Ilyaskina D, Karp T Mar Drugs. 2021; 19(12).

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Chan J, Wang L, Li L, Mu K, Bushek D, Xu Y Front Genet. 2021; 12:795706.

PMID: 34925467 PMC: 8678459. DOI: 10.3389/fgene.2021.795706.

References

Kishore U, Strong P, Perdikoulis M, Reid K . A recombinant homotrimer, composed of the alpha helical neck region of human surfactant protein D and C1q B chain globular domain, is an inhibitor of the classical complement pathway. J Immunol. 2000; 166(1):559-65. DOI: 10.4049/jimmunol.166.1.559. View

Bobak D, Gaither T, Frank M, Tenner A . Modulation of FcR function by complement: subcomponent C1q enhances the phagocytosis of IgG-opsonized targets by human monocytes and culture-derived macrophages. J Immunol. 1987; 138(4):1150-6. View

Stuart L, Ezekowitz R . Phagocytosis: elegant complexity. Immunity. 2005; 22(5):539-50. DOI: 10.1016/j.immuni.2005.05.002. View

Huang S, Yuan S, Guo L, Yu Y, Li J, Wu T . Genomic analysis of the immune gene repertoire of amphioxus reveals extraordinary innate complexity and diversity. Genome Res. 2008; 18(7):1112-26. PMC: 2493400. DOI: 10.1101/gr.069674.107. View

Tirape A, Bacque C, Brizard R, Vandenbulcke F, Boulo V . Expression of immune-related genes in the oyster Crassostrea gigas during ontogenesis. Dev Comp Immunol. 2007; 31(9):859-73. DOI: 10.1016/j.dci.2007.01.005. View

Gestal C, Pallavicini A, Venier P, Novoa B, Figueras A . MgC1q, a novel C1q-domain-containing protein involved in the immune response of Mytilus galloprovincialis. Dev Comp Immunol. 2010; 34(9):926-34. DOI: 10.1016/j.dci.2010.02.012. View

Wang L, Wang L, Yang J, Zhang H, Huang M, Kong P . A multi-CRD C-type lectin with broad recognition spectrum and cellular adhesion from Argopectenirradians. Dev Comp Immunol. 2011; 36(3):591-601. DOI: 10.1016/j.dci.2011.10.002. View

Liu W, Han F, Zhang X . Ran GTPase regulates hemocytic phagocytosis of shrimp by interaction with myosin. J Proteome Res. 2009; 8(3):1198-206. DOI: 10.1021/pr800840x. View

Sellar G, Blake D, Reid K . Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q. Biochem J. 1991; 274 ( Pt 2):481-90. PMC: 1150164. DOI: 10.1042/bj2740481. View

10.

Fujita T . Evolution of the lectin-complement pathway and its role in innate immunity. Nat Rev Immunol. 2002; 2(5):346-53. DOI: 10.1038/nri800. View

11.

Fujita T, Matsushita M, Endo Y . The lectin-complement pathway--its role in innate immunity and evolution. Immunol Rev. 2004; 198:185-202. DOI: 10.1111/j.0105-2896.2004.0123.x. View

12.

Kishore U, Gaboriaud C, Waters P, Shrive A, Greenhough T, Reid K . C1q and tumor necrosis factor superfamily: modularity and versatility. Trends Immunol. 2004; 25(10):551-61. DOI: 10.1016/j.it.2004.08.006. View

13.

Dodds A, Matsushita M . The phylogeny of the complement system and the origins of the classical pathway. Immunobiology. 2007; 212(4-5):233-43. DOI: 10.1016/j.imbio.2006.11.009. View

14.

Tahtouh M, Croq F, Vizioli J, Sautiere P, Van Camp C, Salzet M . Evidence for a novel chemotactic C1q domain-containing factor in the leech nerve cord. Mol Immunol. 2008; 46(4):523-31. DOI: 10.1016/j.molimm.2008.07.026. View

15.

Yu Y, Huang H, Wang Y, Yu Y, Yuan S, Huang S . A novel C1q family member of amphioxus was revealed to have a partial function of vertebrate C1q molecule. J Immunol. 2008; 181(10):7024-32. DOI: 10.4049/jimmunol.181.10.7024. View

16.

Kishore U, Leigh L, Eggleton P, Strong P, Perdikoulis M, Willis A . Functional characterization of a recombinant form of the C-terminal, globular head region of the B-chain of human serum complement protein, C1q. Biochem J. 1998; 333 ( Pt 1):27-32. PMC: 1219551. DOI: 10.1042/bj3330027. View

17.

Cheng S, Zhan W, Xing J, Sheng X . Development and characterization of monoclonal antibody to the lymphocystis disease virus of Japanese flounder Paralichthys olivaceus isolated from China. J Virol Methods. 2006; 135(2):173-80. DOI: 10.1016/j.jviromet.2006.03.016. View

18.

Kumar S, Tamura K, Nei M . MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform. 2004; 5(2):150-63. DOI: 10.1093/bib/5.2.150. View

19.

Yang J, Qiu L, Wei X, Wang L, Wang L, Zhou Z . An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion. Dev Comp Immunol. 2010; 34(12):1274-82. DOI: 10.1016/j.dci.2010.07.004. View

20.

Zhang H, Song X, Wang L, Kong P, Yang J, Liu L . AiCTL-6, a novel C-type lectin from bay scallop Argopecten irradians with a long C-type lectin-like domain. Fish Shellfish Immunol. 2010; 30(1):17-26. DOI: 10.1016/j.fsi.2009.12.019. View