{"title":"利用金标记新糖蛋白定位克氏锥虫的糖结合蛋白。","authors":"J Degett, T Souto-Padron, W De Souza","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Neoglycoproteins labeled with colloidal gold particles were used for the ultrastructural localization of sugar-binding sites in epimastigote, amastigote and trypomastigote forms of Trypanosoma cruzi. Binding sites for N-acetyl-D-glucosamine and D-galactose were seen on the surface of about 80% and 5 to 10% of the trypomastigote forms, respectively. They were inhibited by addition of the respective monosaccharides to the incubation medium. Binding sites for D-mannose were not observed in trypomastigotes. No labeling of the surface of amastigote and epimastigote forms was observed with the neoglycoproteins which bind to N-acetyl-D-glucosamine, D-galactose and D-mannose-binding sites. Labeling of the nucleus and the kinetoplast with the neoglycoprotein which recognizes N-acetyl-D-glucosamine binding sites was observed. The results obtained are discussed in relation to the possible role which surface sugar binding sites play in the process of T. cruzi-host cell interaction.</p>","PeriodicalId":77265,"journal":{"name":"Microscopia electronica y biologia celular : organo oficial de las Sociedades Latinoamericana de Microscopia Electronica e Iberoamericana de Biologia Celular","volume":"14 1","pages":"11-7"},"PeriodicalIF":0.0000,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Localization of sugar-binding proteins in Trypanosoma cruzi using gold-labeled neoglycoproteins.\",\"authors\":\"J Degett, T Souto-Padron, W De Souza\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Neoglycoproteins labeled with colloidal gold particles were used for the ultrastructural localization of sugar-binding sites in epimastigote, amastigote and trypomastigote forms of Trypanosoma cruzi. Binding sites for N-acetyl-D-glucosamine and D-galactose were seen on the surface of about 80% and 5 to 10% of the trypomastigote forms, respectively. They were inhibited by addition of the respective monosaccharides to the incubation medium. Binding sites for D-mannose were not observed in trypomastigotes. No labeling of the surface of amastigote and epimastigote forms was observed with the neoglycoproteins which bind to N-acetyl-D-glucosamine, D-galactose and D-mannose-binding sites. Labeling of the nucleus and the kinetoplast with the neoglycoprotein which recognizes N-acetyl-D-glucosamine binding sites was observed. The results obtained are discussed in relation to the possible role which surface sugar binding sites play in the process of T. cruzi-host cell interaction.</p>\",\"PeriodicalId\":77265,\"journal\":{\"name\":\"Microscopia electronica y biologia celular : organo oficial de las Sociedades Latinoamericana de Microscopia Electronica e Iberoamericana de Biologia Celular\",\"volume\":\"14 1\",\"pages\":\"11-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1990-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Microscopia electronica y biologia celular : organo oficial de las Sociedades Latinoamericana de Microscopia Electronica e Iberoamericana de Biologia Celular\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Microscopia electronica y biologia celular : organo oficial de las Sociedades Latinoamericana de Microscopia Electronica e Iberoamericana de Biologia Celular","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
用胶体金标记的新糖蛋白对克氏锥虫的拟马乳突体、无马乳突体和锥乳突体进行糖结合位点的超微结构定位。n -乙酰- d -葡萄糖胺和d -半乳糖的结合位点分别出现在约80%和5 - 10%的锥马鞭毛虫的表面。通过在培养液中添加相应的单糖来抑制它们。d -甘露糖的结合位点未在密乳线虫中观察到。未观察到与n -乙酰- d -氨基葡萄糖、d -半乳糖和d -甘露糖结合位点结合的新糖蛋白在无马鞭毛石和副马鞭毛石形态表面的标记。观察到用识别n -乙酰- d -氨基葡萄糖结合位点的新糖蛋白标记细胞核和着丝体。讨论了表面糖结合位点在克氏绦虫与宿主细胞相互作用过程中可能起的作用。
Localization of sugar-binding proteins in Trypanosoma cruzi using gold-labeled neoglycoproteins.
Neoglycoproteins labeled with colloidal gold particles were used for the ultrastructural localization of sugar-binding sites in epimastigote, amastigote and trypomastigote forms of Trypanosoma cruzi. Binding sites for N-acetyl-D-glucosamine and D-galactose were seen on the surface of about 80% and 5 to 10% of the trypomastigote forms, respectively. They were inhibited by addition of the respective monosaccharides to the incubation medium. Binding sites for D-mannose were not observed in trypomastigotes. No labeling of the surface of amastigote and epimastigote forms was observed with the neoglycoproteins which bind to N-acetyl-D-glucosamine, D-galactose and D-mannose-binding sites. Labeling of the nucleus and the kinetoplast with the neoglycoprotein which recognizes N-acetyl-D-glucosamine binding sites was observed. The results obtained are discussed in relation to the possible role which surface sugar binding sites play in the process of T. cruzi-host cell interaction.