Chicken lung lectin is a functional C-type lectin and inhibits haemagglutination by influenza A virus
Chicken lung lectin is a functional C-type lectin and inhibits haemagglutination by influenza A virus
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DOI：
10.1016/j.vetmic.2007.12.008
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发表时间：
2008-07-27
影响因子：
3.3
通讯作者：
Haagsman, Henk P.
中科院分区：
文献类型：
--
作者：
Hogenkamp, Astrid;Isohadouten, Najiha;Haagsman, Henk P.
钙依赖性（C型）凝集素家族的许多蛋白质已被证明在先天免疫中发挥重要作用。它们可以与各种碳水化合物结合，这使它们能够与微生物表面上存在的配体相互作用。我们以前报道了一种新的推定的鸡凝集素，这是主要定位于呼吸道，因此被称为鸡肺凝集素（cLL）的发现。为了研究cLL的生物化学和生物物理特性，对重组蛋白进行了表达、亲和纯化和鉴定。重组cLL表达为四种不同大小的肽，这很可能是由于翻译后修饰。蛋白质的交联导致形成两种高分子量产物，这表明cLL形成三聚体，甚至可能形成多聚体亚基。cLL显示具有凝集素活性，以钙依赖性方式优先结合α-甘露糖。此外，cLL显示出抑制甲型流感病毒亚型H3 N2和H1N1的人分离株的血凝活性。这些结果表明，cLL是一种真正的C型凝集素，具有非常明显的糖特异性，这种鸡凝集素可能在天然免疫中发挥重要作用。(c)2008年由Elsevier B. V.出版。
Many proteins of the calcium-dependent (C-type) lectin family have been shown to play an important role in innate immunity. They can bind to a broad range of carbohydrates, which enables them to interact with ligands present on the surface of micro-organisms. We previously reported the finding of a new putative chicken lectin, which was predominantly localized to the respiratory tract, and thus termed chicken lung lectin (cLL). In order to investigate the biochemical and biophysical properties of cLL, the recombinant protein was expressed, affinity purified and characterized. Recombinant cLL was expressed as four differently sized peptides, which is most likely due to post-translational modification. Crosslinking of the protein led to the formation of two high-molecular weight products, indicating that cLL forms trimeric and possibly even multimeric subunits. cLL was shown to have lectin activity, preferentially binding to a-mannose in a calcium-dependent manner. Furthermore, cLL was shown to inhibit the haemagglutination-activity of human isolates of influenza A virus, subtype H3N2 and H1N1. These result show that cLL is a true C-type lectin with a very distinct sugar specificity, and that this chicken lectin could play an important role in innate immunity. (c) 2008 Published by Elsevier B.V.