{"title":"寄生虫凝集素:不仅仅是粘附分子?","authors":"E. A. M. Silva, Thaís Viana Fialho Martins","doi":"10.4172/2168-958X.1000120","DOIUrl":null,"url":null,"abstract":"Several studies demonstrate the involvement of lectins in the recognition of carbohydrates present on the surface of different kinds of pathogens [1-3], including parasites of the genus Leishmania [4,5]. The recognition often involves the modulation of the host immune response due to the activation of signaling pathways initiated by the stimulation of lectins present on the surface of cells from immune system by carbohydrates from pathogens [1,2]. On the other hand, lectins from microorganisms are also involved in infections: HeparinBinding Protein (HBP) from Trypanosoma cruzi are involved in processes of amastigote and epimastigotes adhesion to the mammalian host cells and to the intestinal epithelium of insects, respectively [6-8]. Furthermore, galactose/N-acetylgalactosamine (Gal/GalNAc) lectin is involved in the infection by Entamoeba histolytica, responsible for the third highest number of death from parasitic diseases in the world [9-11]. Other relevant lectins from parasites are involved in mediating protozoa attachment to the host cells, acting as valuable tools to study pathogenesis of infection: mannose lectin (MBP) from Acanthamoeba, causative agent of keratitis, mediates parasite adhesion to the host cells, and may serve as a marker of pathogenicity of this parasite; micronemal protein (MIC1), a Toxoplasma gondii adhesin, bind to host sialic acid moieties, playing role in the parasite invasion and virulence; Tritrichomonas foetus lectin (TFL), a sialic acid specific lectin, is involved in mucosal surface attachment and immunogenicity of Tritrichomonas foetus, a protozoan parasite of the bovine urogenital tract; and Cryptosporidium parvum Clec (CpClec), a novel mucin-like glycoprotein with a C-type lectin domain (CTLD), is involved in Cryptosporidium-host cell interactions [12].","PeriodicalId":92404,"journal":{"name":"Journal of glycobiology","volume":"114 1","pages":"1-2"},"PeriodicalIF":0.0000,"publicationDate":"2016-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Parasite Lectins: More than Adhesion Molecules?\",\"authors\":\"E. 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Furthermore, galactose/N-acetylgalactosamine (Gal/GalNAc) lectin is involved in the infection by Entamoeba histolytica, responsible for the third highest number of death from parasitic diseases in the world [9-11]. 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引用次数: 1
摘要
几项研究表明,凝集素参与识别存在于不同种类病原体表面的碳水化合物[1-3],包括利什曼原虫属寄生虫[4,5]。来自病原体的碳水化合物刺激免疫系统细胞表面的凝集素,从而激活信号通路,这种识别通常涉及宿主免疫反应的调节[1,2]。另一方面,来自微生物的凝集素也参与了感染:克氏锥虫的肝素结合蛋白(HeparinBinding Protein, HBP)分别参与了无尾马鞭毛体与哺乳动物宿主细胞和昆虫肠上皮的粘附过程[6-8]。此外,半乳糖/ n -乙酰半乳糖胺(Gal/GalNAc)凝集素与溶组织内阿米巴感染有关,而溶组织内阿米巴是世界上因寄生虫病死亡人数第三高的疾病[9-11]。来自寄生虫的其他相关凝集素参与介导原生动物附着于宿主细胞,是研究感染发病机制的有价值的工具:角膜炎病原体棘阿米巴的甘露糖凝集素(MBP)介导寄生虫附着于宿主细胞,并可作为该寄生虫致病性的标志;刚地弓形虫黏附蛋白MIC1与宿主唾液酸部分结合,参与了弓形虫的入侵和毒力;三毛单胞菌胎儿凝集素(Tritrichomonas foetus lectin, TFL)是一种唾液酸特异性凝集素,参与牛泌尿生殖道原生寄生虫胎儿三毛单胞菌的粘膜表面附着和免疫原性;小隐孢子虫Clec (CpClec)是一种具有c型凝集素结构域(CTLD)的新型黏液样糖蛋白,参与隐孢子虫与宿主细胞的相互作用[12]。
Several studies demonstrate the involvement of lectins in the recognition of carbohydrates present on the surface of different kinds of pathogens [1-3], including parasites of the genus Leishmania [4,5]. The recognition often involves the modulation of the host immune response due to the activation of signaling pathways initiated by the stimulation of lectins present on the surface of cells from immune system by carbohydrates from pathogens [1,2]. On the other hand, lectins from microorganisms are also involved in infections: HeparinBinding Protein (HBP) from Trypanosoma cruzi are involved in processes of amastigote and epimastigotes adhesion to the mammalian host cells and to the intestinal epithelium of insects, respectively [6-8]. Furthermore, galactose/N-acetylgalactosamine (Gal/GalNAc) lectin is involved in the infection by Entamoeba histolytica, responsible for the third highest number of death from parasitic diseases in the world [9-11]. Other relevant lectins from parasites are involved in mediating protozoa attachment to the host cells, acting as valuable tools to study pathogenesis of infection: mannose lectin (MBP) from Acanthamoeba, causative agent of keratitis, mediates parasite adhesion to the host cells, and may serve as a marker of pathogenicity of this parasite; micronemal protein (MIC1), a Toxoplasma gondii adhesin, bind to host sialic acid moieties, playing role in the parasite invasion and virulence; Tritrichomonas foetus lectin (TFL), a sialic acid specific lectin, is involved in mucosal surface attachment and immunogenicity of Tritrichomonas foetus, a protozoan parasite of the bovine urogenital tract; and Cryptosporidium parvum Clec (CpClec), a novel mucin-like glycoprotein with a C-type lectin domain (CTLD), is involved in Cryptosporidium-host cell interactions [12].