A novel C1q domain containing protein in black rockfish (Sebastes schlegelii) serves as a pattern recognition receptor with immunoregulatory properties and possesses binding activity to heat-aggregated IgG
A novel C1q domain containing protein in black rockfish (Sebastes schlegelii) serves as a pattern recognition receptor with immunoregulatory properties and possesses binding activity to heat-aggregated IgG
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黑石斑鱼 (Sebastes schlegelii) 中含有新型 C1q 结构域的蛋白质可作为具有免疫调节特性的模式识别受体,并具有与热聚集 IgG 的结合活性
DOI:
10.1016/j.fsi.2019.01.004
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发表时间:
2019-04-01
影响因子:
4.7
通讯作者:
Hu, Yong-hua
中科院分区:
文献类型:
--
作者:
Du, Xue;Wang, Guang-hua;Hu, Yong-hua
C1q-domain-containing (C1qDC) proteins, which are involved in a series of immune responses, are important pattern recognition receptors in innate immunity in vertebrates and invertebrates. Functional studies of C1qDC proteins in vertebrates are scarce. In the present study, a C1qDC protein (SsC1qDC) from the teleost black rockfish (Sebastes schlegelii) was identified and examined at expression and functional levels. The open reading frame of SsC1qDC is 636 bp, and the predicted amino acid sequence of SsC1qDC shares 62%-69% overall identity with the C1qDC proteins of several fish species. SsC1qDC possesses conserved C1qDC features, including a signal sequence and a C1q domain. SsClqDC was expressed in different tissues and its expression was upregulated by bacterial and viral infection. Recombinant SsC1qDC (rSsC1qDC) exhibited apparent binding activities against PAMPs including LPS and PGN. rSsC1qDC had antibacterial activity against Vibrio parehaemolyticus, and was able to enhance the phagocytic activity of macrophages towards Vibrio anguillarwn. rSsC1qDC interacted with human heat-aggregated IgG. Furthermore, in the presence of rSsC1qDC, fish exhibited enhanced resistance against bacterial infection. Collectively, these results indicated that SsC1qDC serves as a pattern recognition receptor and plays a vital role in the defense system of black rockfish.