Bonura Angela, Vizzini Aiti, Salerno Giuseppina, Parrinello Nicolò, Longo Valeria, Colombo Paolo
Istituto di Biomedicina ed Immunologia Molecolare Alberto Monroy del Consiglio Nazionale delle Ricerche, Via Ugo La Malfa 153, Palermo, Italy.
Mol Immunol. 2009 Jul;46(11-12):2389-94. doi: 10.1016/j.molimm.2009.04.035. Epub 2009 May 29.
Collectins are a family of calcium-dependent lectins that are characterized by their collagen-like domains. Considerable interest has been focused on this class of proteins because of their ability to interact with components of the complement system activating a cascade of events responsible for the activation of the innate immune system. A differential screening between LPS-challenged and naïve Ciona intestinalis has been performed allowing the isolation of a full length cDNA encoding for a 221 AA protein. In silico analysis has shown that this polypeptide displays protein domains with similarities to mannose-binding lectins. A phylogenetic analysis suggested that C. intestinalis MBL has evolved early as a prototype of vertebrate MBL. Real-time PCR assay demonstrated that this gene is strongly activated after LPS injection in the tunica. In situ hybridization performed in LPS-induced animals has shown that this gene is expressed in granular amoebocytes and large granules hemocytes in the inflamed body wall tissue. Finally, an antimicrobial activity of the C. intestinalis MBL has been demonstrated.
凝集素是一类钙依赖性凝集素，其特征在于具有胶原样结构域。由于它们能够与补体系统的成分相互作用，激活一系列负责先天免疫系统激活的事件，因此这类蛋白质受到了广泛关注。我们对经脂多糖（LPS）刺激的和未受刺激的玻璃海鞘进行了差异筛选，从而分离出了一个编码221个氨基酸蛋白质的全长cDNA。计算机分析表明，该多肽显示出与甘露糖结合凝集素相似的蛋白质结构域。系统发育分析表明，玻璃海鞘的甘露糖结合凝集素（MBL）作为脊椎动物MBL的原型进化得较早。实时PCR分析表明，在体壁中注射LPS后，该基因被强烈激活。在LPS诱导的动物中进行的原位杂交表明，该基因在发炎体壁组织中的颗粒变形细胞和大颗粒血细胞中表达。最后，已证明玻璃海鞘MBL具有抗菌活性。
