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A novel multi-domain C1qDC protein from Zhikong scallop Chlamys farreri provides new insights into the function of invertebrate C1qDC proteins
Wang, Leilei1,3,4; Wang, Lingling1; Zhang, Daoxiang1,3; Jiang, Qiufen1,3; Sun, Rui1,3; Wang, Hao1; Zhang, Huan1; Song, Linsheng2
2015-10-01
Source PublicationDEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume52Issue:2Pages:202-214
SubtypeArticle
AbstractThe C1q domain containing (C1qDC) proteins are a family of proteins possessing globular CM (gC1q) domains, and they rely on this domain to recognize various ligands such as PAMPs, immunoglobulins, ligands on apoptotic cell. In the present study, a novel multi-domain C1qDC protein (CfC1qDC-2) was identified from scallop Chlamys farreri, and its full length cDNA was composed of 1648 bp, encoding a signal peptide and three typical gC1q domains. BLAST analysis revealed significant sequence similarity between CfC1 qDC-2 and C1qDC proteins from mollusks. Three gC1q domains were predicted in its tertiary structure to form a tightly packed bell-shaped trimer, and each one adopted a typical 10-stranded sandwich fold with a jelly-roll topology and contained six aromatic amino acids forming the hydrophobic core. The mRNA transcripts of CfC1qDC-2 were mainly detected in the tissues of hepatopancreas and gonad of adult scallops, and the expression level was up-regulated in hemocytes after stimulated by LPS, PGN and beta-glucan. During the embryonic development of scallop, the mRNA transcripts of CfC1qDC-2 were presented in all the detected stages, and the expression level was up-regulated from D-hinged larvae and reached the highest at eye-spot larvae. The recombinant protein of MBP-CfC1 qDC-2 (rCfC1qDC-2) could bind various PAMPs including LPS, PGN, LTA, beta-glucan, mannan as well as polyl:C, and different microorganisms including three Gram-negative bacteria, three Gram-positive bacteria and two yeasts, as well as scallop apoptotic cells. Meanwhile, rCfC1qDC-2 could interact with human heat-aggregated IgG and IgM, and inhibit the C1q-dependent hemolysis of rabbit serum. All these results indicated that CfC1qDC-2 could recognize not only PAMPs as a PRR, but also the apoptotic cells. Moreover, the similar structures and functions shared by CfC1qDC-2 and complement C1q provided a new insight into the evolution of C1qDC proteins in complement system. (C) 2015 Elsevier Ltd. All rights reserved.
KeywordC1qdc Proteins Immune Recognition Immunoglobulin Binding Apoptotic Cell Binding
DOI10.1016/j.dci.2015.05.009
Indexed BySCI
Language英语
WOS IDWOS:000360592200011
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Cited Times:9[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/50772
Collection实验海洋生物学重点实验室
Affiliation1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Dalian Ocean Univ, Dalian 116023, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
4.Lianyungang Maternal & Child Hlth Hosp, Lianyungang 222001, Peoples R China
First Author AffilicationKey Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
Recommended Citation
GB/T 7714
Wang, Leilei,Wang, Lingling,Zhang, Daoxiang,et al. A novel multi-domain C1qDC protein from Zhikong scallop Chlamys farreri provides new insights into the function of invertebrate C1qDC proteins[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2015,52(2):202-214.
APA Wang, Leilei.,Wang, Lingling.,Zhang, Daoxiang.,Jiang, Qiufen.,Sun, Rui.,...&Song, Linsheng.(2015).A novel multi-domain C1qDC protein from Zhikong scallop Chlamys farreri provides new insights into the function of invertebrate C1qDC proteins.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,52(2),202-214.
MLA Wang, Leilei,et al."A novel multi-domain C1qDC protein from Zhikong scallop Chlamys farreri provides new insights into the function of invertebrate C1qDC proteins".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 52.2(2015):202-214.
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