蛇毒C-型凝集素研究进展

蛇毒中含有丰富的非酶活性C－型凝集素蛋白,根据其结构及功能的差异,该类蛋白可分为Ca^2 依赖的有糖基识别活性的C－型真凝集素及无糖基识别活性的C－型凝集素样蛋白。C－型真凝集素的结构相似度高,而功能却较为单一,具有特异性糖结合活性;C－型凝集样蛋白的结构变异度大,活性亦具有多样性。后者能通过特异性的蛋白质－蛋白质相互作用而作用于血液凝固系统及血小板,从而发挥抗凝或促凝的生理功能。     

哺乳类C型凝集素超级家族

C型凝集素超级家族根据其糖识别域(CRD)的一级结构分为蛋白聚糖、Ⅱ型跨膜受体、胶原凝素、选凝素、自然杀伤细胞受体及多CRDⅠ型跨膜受体等6个家族. 每一家族的成员具有同源的氨基酸序列、相同的总体分子结构及类似的生物学功能.从CRD的一级结构至三级结构水平确定了C型凝集素选择性糖识别的分子基础.     

病毒感染和免疫清除中的C型凝集素

树突状细胞和朗罕氏细胞是人体防御病毒入侵的第一道屏障,这些细胞表达的C型凝集素对于细胞发挥抗原免疫清除和细胞之间的黏附有重要作用。其中DC—SIGN和DC—SIGNR在HIV等多种病毒的感染中发挥重要作用。随着基因组学的发展鉴定了许多新的C型凝集素,它们在免疫清除和病毒感染中都可能发挥重要作用。     

C型凝集素受体与抗真菌免疫

Toll样受体(TLR)的发现为研究病原生物的识别和免疫应答的起始开辟了新的视角,然而近期研究发现"非-TLR"受体在该过程尤其在抗真菌免疫中亦起着重要作用.其中研究甚为活跃的是C型凝集素受体(CLR)家族的一些成员,包括甘露糖受体、DC-SIGN、Dectin-1、Dectin-2及胶原凝集素.本文对这些受体在真菌识别、摄取、杀伤及其在宿主免疫反应的诱导和调节中所发挥的作用予以综述.     

蛇毒C型凝集素类蛋白cDNA与基因组DNA序列分析显示特别的转录后加工(英文)

为研究蛇毒C型凝集素类蛋白的快速进化机制和结构功能关系 ,使用PCR技术扩增了若干编码C型凝集素类蛋白 β链的cDNA分子以及agkisasinβ的基因组DNA ,并将这些扩增产物进行克隆和测序 .对测序结果与试验过程中的具体条件进行了因果关系分析 ,并且进行点阵图比较和多序列比对 .结果表明 ,可能存在“转录后同源重组”等转录后的事件 ,在蛇毒C型凝集素类蛋白的多样性上起着重要的作用 .对于解释基因数目与蛋白质数目的差异这一后基因组时代的重要问题 ,具有一定的参考价值 .首次报告蛇毒C型凝集素类蛋白的基因组DNA序列 ,其中未发现有内含子     

半乳糖凝集素的结构和功能

半乳糖凝集素的结构和功能关键词半乳糖凝集素凝集素是能与特定糖结构结合的蛋白质,能够识别广泛分布于动物组织中的糖复合物。动物凝集素可分为４类：Ｃ类凝集素（包括选择蛋白,Ｓｅｌｅｃｔｉｎ）、Ｐ类凝集素、正五聚蛋白（Ｐｅｎｔｒａｘｉｎｓ）和半乳糖凝集素（暂...     

伊蚊C型凝集素mosGCTL-2是登革病毒感染相关的重要蛋白质

C型凝集素是一类含有糖结合结构域的蛋白质,从节肢动物到哺乳动物的C型凝集素都具有共同的基序,它在进化上相当保守,在免疫反应中发挥重要作用. 埃及伊蚊表达30多种C型凝集素蛋白,它是登革病毒的关键传播媒介,这些蛋白质对病毒和细菌感染均有至关重要的作用. 最近研究表明,C型凝集素mosGCTL-3与二型登革热病毒包膜蛋白具有相互作用,能够增强登革病毒对埃及伊蚊的感染. 在本文中,我们发现了C型凝集素蛋白mosGCTL-2具有与mosGCTL-3类似的功能. 两种C型凝集素mosGCTL-2和mosGCTL-3的氨基酸残基序列一致性高达43.56％. 为研究mosGCTL-2在登革病毒蚊媒传播中的作用,我们通过果蝇S2细胞表达系统表达纯化了mosGCTL-2蛋白. 结果表明,mosGCTL-2与二型登革热病毒包膜蛋白的结合具有钙离子依赖性. 进一步的研究表明,埃及伊蚊感染登革病毒能够诱导mosGCTL2表达上调,是二型登革热病毒感染埃及伊蚊所必需的蛋白质. 以上研究说明,mosGCTL-2蛋白可能是在登革热病毒感染埃及伊蚊中起重要作用的一种模式识别受体.     

豆科凝集素研究进展

豆科凝集素是植物凝集素中最丰富,也是研究最多的一类凝集素。在生理条件下豆科凝集素大多是以二聚体或四聚体的形式存在,这种低聚物的形式给予豆科凝集素较强的糖专一性和大分子结构的稳定性。豆科凝集素除作为植物储存物质的作用外,还具有识别糖蛋白、糖肽及生物膜中碳水化合物和作为植物与微生物的共生介质等生理功能。现对豆科凝集素的结构、功能及其在生物学、农业和医学方面的应用进行了综述。     

糖类模式识别分子纤维胶凝蛋白与补体凝集素活化途径

纤维胶凝蛋白(ficolin)是一组存在于人、猪、小鼠和海鞘等动物体内,含有胶原样结构域和纤维蛋白原样结构域的糖蛋白。它们的分子结构相似。多形成寡聚体,其基因结构和氨基酸序列有一定的同源性。Ficolin与MBL的功能相似,识别并特异结合某些糖类,所以它们可能是一种重要的糖类模式识别分子。血清中的ficolin结合病原体表面的糖类配体后,通过调理吞噬作用及凝集素途径激活补体,是天然免疫中的效应分子。本文主要介绍了纤维胶凝蛋白(ficolin)的分子结构、生物学特性及其补体活化的凝集素途径。     

哺乳动物凝集素及其生物学作用

哺乳动物凝集素及其生物学作用周柔丽（北京医科大学细胞生物学教研室,北京１０００８３）关键词动物凝集素,细胞识别自Ａｓｈｗｅｌｌ和Ｍｏｒｅｌｌ发现肝细胞凝集素廿余年来在高等动物体内陆续发现了多种多样的凝集素。其生物学作用涉及到许多重要的生理与病理活动,...     

C-type lectins do not act as functional receptors for filovirus entry into cells

Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.     

Structural and biological characterization of Nattectin, a new C-type lectin from the venomous fish Thalassophryne nattereri

Lectins are glycan-binding receptors that recognize glycan epitopes on foreign pathogens and in the host systems. They can be involved in functions that include innate immunity, development, immune regulation and homeostasis. Several lectins have been purified and characterized from fish species. In this work, using cation-exchange chromatography, a galactose-specific lectin belonging to the family of C-type lectins was isolated from the venom of the Brazilian venomous fish Thalassophryne nattereri. Nattectin is a basic, non-glycosilated, 15 kDa monomeric protein. It exhibits hemagglutination activity that is independent of Ca²⁺. We also demonstrated a lectin activity for Nattectin in the innate immune system, especially in neutrophil mobilization in mice, indicating that marine organisms are source of immunomodulator agents.     

C-type lectin OCILRP2/Clr-g and its ligand NKRP1f costimulate T cell proliferation and IL-2 production

We are reporting the identification of a novel C-type lectin receptor-ligand pair that is involved in T cell costimulation. The receptor, OCILRP2/Clr-g, is rapidly induced following T cell activation and maintained at a substantial level of up to 72 h. The ligand, NKRP1f, is predominantly expressed on dendritic cells (DC). The soluble OCILRP2-Ig blocking protein significantly suppresses specific antigen-stimulated T cell proliferation as well as IL-2 secretion both in vitro and in vivo; conversely, NKRP1f-expressing antigen presenting cells (APC) enhance B7.1/CD28-mediated costimulation for T cell proliferation through interaction with OCILRP2/Clr-g. Our studies reveal a unique functional interaction between two C-type lectins, OCILRP2/Clr-g and NKRP1f, during APC-mediated T cell costimulation and suggest a role for C-type lectins in maintaining T cell response or memory in vivo.     

Primary structure characterization of Bothrops jararacussu snake venom lectin

The complete amino acid sequence of the lectin from Bothrops jararacussu snake venom (BJcuL) is reported. The sequence was determined by Edman degradation and amino acid analysis of the S-carboxymethylated BJcuL derivative (RC-BJcuL) and from its peptides originated from enzymatic digestion. The sequence of amino acid residues showed that this lectin displays the invariant amino acid residues characterized in C-type lectins. Amino acids analysis revealed a high content of acidic amino acids and leucine. These findings suggest that BJcuL, like other snake venom lectins, possesses structural similarities to the carbohydrate recognition domain (CRD) of calcium-dependent animal lectins belonging to the C-type -galactoside binding lectin family.     

Immune-related, lectin-like receptors are differentially expressed in the myeloid and lymphoid lineages of zebrafish

The identification of C-type lectin (Group V) natural killer (NK) cell receptors in bony fish has remained elusive. Analyses of the Fugu rubripes genome database failed to identify Group V C-type lectin domains (Zelensky and Gready, BMC Genomics 5:51, 2004) suggesting that bony fish, in general, may lack such receptors. Numerous Group II C-type lectin receptors, which are structurally similar to Group V (NK) receptors, have been characterized in bony fish. By searching the zebrafish genome database we have identified a multi-gene family of Group II immune-related, lectin-like receptors (illrs) whose members possess inhibiting and/or activating signaling motifs typical of Group V NK receptors. Illr genes are differentially expressed in the myeloid and lymphoid lineages, suggesting that they may play important roles in the immune functions of multiple hematopoietic cell lineages.