文昌鱼中一种具有细菌凝集和结合活性的含LDLa结构域的新型C型凝集素。
A new LDLa domain-containing C-type lectin with bacterial agglutinating and binding activity in amphioxus.
作者信息
Qu Baozhen, Yang Shuangshuang, Ma Zengyu, Gao Zhan, Zhang Shicui
机构信息
Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity, Qingdao 266003, China; Department of Marine Biology, Ocean University of China, Qingdao 266003, China.
Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity, Qingdao 266003, China; Department of Marine Biology, Ocean University of China, Qingdao 266003, China.
出版信息
Gene. 2016 Dec 15;594(2):220-228. doi: 10.1016/j.gene.2016.09.009. Epub 2016 Sep 6.
Over 1200 C-type lectin gene models have been identified in amphioxus, but only a few of them have been functionally characterized. In this study, we identified a C-type lectin, BjCTL, with domain structure of LDLa-CTLD-EGF_Lam, the first such data in chordates. It was expressed mainly in the notochord and ovary in a tissue-dependent fashion. Recombinant BjCTL was characterized as a typical Ca-dependent carbohydrate-binding protein capable of agglutinating and binding to both Gram-negative and positive bacteria we tested. In addition, it specifically bound to insoluble lipopolysaccharide, lipoteichoic acid and peptidoglycan, which can be inhibited by galactose. We also showed that the interaction of BjCTL with the bacteria is primarily attributable to CTLD domain. Thus, BjCTL is a novel pattern recognition protein involved in lectin-mediated innate immunity.
在文昌鱼中已鉴定出1200多个C型凝集素基因模型，但其中只有少数几个在功能上得到了表征。在本研究中，我们鉴定了一种C型凝集素BjCTL，其结构域结构为LDLa-CTLD-EGF_Lam，这是脊索动物中的首个此类数据。它主要以组织依赖的方式在脊索和卵巢中表达。重组BjCTL被表征为一种典型的钙依赖性碳水化合物结合蛋白，能够凝集并结合我们测试的革兰氏阴性菌和阳性菌。此外，它特异性结合不溶性脂多糖、脂磷壁酸和肽聚糖，而这些均可被半乳糖抑制。我们还表明，BjCTL与细菌的相互作用主要归因于CTLD结构域。因此，BjCTL是一种参与凝集素介导的固有免疫的新型模式识别蛋白。
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