Characterization of complement 1q binding protein of tiger shrimp, Penaeus monodon, and its C1q binding activity

文献类型： 外文期刊

第一作者： Yang, Lishi

作者： Yang, Lishi;Liu, Xianjun;Liu, Wenjing;Li, Xiaolan;Qiu, Lihua;Huang, Jianhua;Jiang, Shigui;Liu, Xianjun;Liu, Wenjing;Li, Xiaolan

作者机构：

关键词： C1qBP/gC1qR/p33;Penaeus monodon;Vibrio vulnificus;Innate immunity;Native protein;Complement component

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.581； 五年影响因子：4.851 ）

ISSN： 1050-4648

年卷期： 2013 年 34 卷 1 期

页码：

收录情况： SCI

摘要： The receptor for the globular heads of C1q, C1qBP/gC1qR/p33, is a multicompartmental, multifunctional cellular protein with an important role in infection and in inflammation. In the present study, we identified and characterized the complement component 1q subcomponent binding protein (C1qBP) from the tiger shrimp Penaeus monodon (designated as PmC1qBP). The open reading frame of PmC1qBP encodes 262 amino acid residues with a conserved MAM33 domain, an arginine-glycine-aspartate cell adhesion motif, and a mitochondrial targeting sequence in the first 53 amino acids. PmC1qBP shares 32%-81% similarity with known C1qBPs and clusters with lobster gC1qR under phylogenetic analysis. The temporal PmC1qBP mRNA expression in the hepatopancreas was significantly enhanced at 9 h after Vibrio vulnificus challenge. The native PmC1qBP was expressed in the gills, hepatopancreas, ovaries, and intestines as a precursor (38 kDa) and the active peptide (35 kDa). The recombinant PmC1qBP protein was expressed in Escherichia coli BL21, and was purified using nickel-nitrilotriacetic acid agarose. A complement 1q binding assay indicated that the rC1qBP protein competitively binds to C1q in mouse serum. The data reveal that PmC1qBP is not only involved in shrimp immune responses to pathogenic infections, but also cross-binding to the mouse C1q. (c) 2012 Elsevier Ltd. All rights reserved.

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