A new LDLa domain-containing C-type lectin with bacterial agglutinating and binding activity in amphioxus
A new LDLa domain-containing C-type lectin with bacterial agglutinating and binding activity in amphioxus
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DOI：
10.1016/j.gene.2016.09.009
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发表时间：
2016-12-15
期刊：
影响因子：
3.5
通讯作者：
Zhang, Shicui
中科院分区：
文献类型：
--
作者：
Qu, Baozhen;Yang, Shuangshuang;Zhang, Shicui
在文昌鱼中已经鉴定了1200多个C型凝集素基因模型，但只有少数几个已被功能鉴定。在这项研究中，我们确定了一个C型凝集素，BjCTL，结构域结构的LDLa-CTLD-EGF_Lam，在脊索动物中的第一个这样的数据。主要在脊索和卵巢中表达，呈组织依赖性。重组BjCTL的特点是作为一个典型的钙依赖性碳水化合物结合蛋白能够凝集和结合革兰氏阴性和阳性细菌，我们测试。此外，它特异性结合不溶性脂多糖，脂磷壁酸和肽聚糖，可以被半乳糖抑制。我们还发现BjCTL与细菌的相互作用主要归因于CTLD结构域。因此，BjCTL是一种新的模式识别蛋白，参与凝集素介导的先天免疫。(C)© 2016 Elsevier B. V.版权所有
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 Ca2+-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. (C) 2016 Elsevier B.V. All rights reserved