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Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors
Glycoconjugate Journal ( IF 3 ) Pub Date : 2023-09-11 , DOI: 10.1007/s10719-023-10129-4
Albert M. Wu

The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N-glycan chains, as well as their polyvalent forms in N-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian N-glycans, including the N-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by Molar Relative Potency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (M5) and Biantennary N-linked core pentasaccharide (MDi) ≥ α1 → 3, α1 → 6 Mannotriose (M3) > Manα1 → 3Man (α1 → 3Mannobiose), Manα1 → 2Man (α1 → 2Mannobiose), Manα1 → 6Man (α1 → 6Mannobiose), Manα1 → 4Man (α1 → 4Mannobiose) > GlcNAcβ1 → 2Man (β1 → 2 N-Acetyl glucosamine-mannose) > Manα1 → /Glcα1 → > Man > Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcβ1 → branches (M3 to M9 / MMono to Penta etc.) and a table of three Manα1 → and Glcα1 → related biomasses of six recognition factors involved in the Con A-glycan interactions has also been demonstrated. These themes should be one of the most valuable advances since 1980s.



中文翻译:

结构单元、糖表位/哺乳动物 N-聚糖在 Con A-聚糖相互作用中的作用、它们的代码和它们的识别因子

80 多年来,Con A 的结合特性已被深入研究并广泛应用于糖复合物/糖生物学。然而,Con A 与这些哺乳动物结构单元、糖表位、N-聚糖链以及参与 Con A-聚糖相互作用的N-糖蛋白中的多价形式的作用和功能关系尚未得到很好的定义和组织。在本研究中,通过我们成熟的方法——酶联凝集素吸附剂(ELLSA)和抑制测定来分析参与这些相互作用的识别因素。基于所有获得的数据,可以得出结论,如之前报道的那样,Con A对Manα1→和Glcα1→相关聚糖具有相对广泛和广泛的识别能力。它不仅与酵母甘露聚糖和糖原反应强烈,而且与大量哺乳动物N-聚糖良好结合,包括大鼠舌下糖蛋白(RSL)、人Tamm-Horsfall糖蛋白(THGP)、甲状腺球蛋白和乳铁蛋白的N-聚糖。 。Con A 对配体的识别特异性,以摩尔相对效力(Molar RP)表示,按递减顺序依次为:α1 → 3、α1 → 6 甘露五糖(M 5 和双触角N连接核心五糖(M Di ) ≥ α1 → 3、α1 → 6 甘露三糖 ( M 3 ) > Manα1 → 3Man (α1 → 3 甘露二糖)、Manα1 → 2Man (α1 → 2 甘露二糖)、Manα1 → 6Man (α1 → 6 甘露二糖)、Manα1 → 4Man (α1 → 4甘二糖) > GlcNAcβ1 → 2 Man (β1 → 2 N-乙酰氨基葡萄糖-甘露糖) > Manα1 → /Glcα1 → >  Man >  Glc,而 Gal / GalNAc 不活跃。此外,在本研究中,Man相关的代码系统建议通过Man和GlcNAcβ1→分支的数量(M 3M 9 / M Mono到Penta等)和三个Manα1→和Glcα1→相关的表来表达参与 Con A-聚糖相互作用的六种识别因子的生物量也已得到证实。这些主题应该是 20 世纪 80 年代以来最有价值的进步之一。

更新日期:2023-09-14
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