{"title":"哺乳动物糖缀合物中GalNAcα1→3/O相关糖基的位点和基序及其凝集素识别作用","authors":"Albert M Wu","doi":"10.1007/s10719-022-10068-6","DOIUrl":null,"url":null,"abstract":"<p><p>Galα1 → and GalNAcα1 → are the two essential key sugars in human blood group AB active glycotopes, in which GalNAcα1 → related sequences are located at both sides of the nonreducing and the reducing ends of human blood group A active O-glycans. It is also found at the nonreducing ends of GlcNAc N-glycans and glycosphingolipid(GSL) of human blood group A active glycotopes (A<sub>h</sub>) and Forssman antigen (F<sub>p</sub>). When monosaccharides and their α, β anomers are involved in basic units to express the complex size of the combining sites of the GalNAcα1 → specific lectins, they can be divided into a cavity site to accommodate the GalNAcα → key sugar and a subsite with a wide and broad range of recognition area to adopt the rest part of sugar sequences or glycotopes. The function of the subsite is assumed to act as an enhancement factor to increase its affinity power. The following three points are the theme of this mini review: (1) the loci and distribution of the GalNAcα1 → related glycotopes in mammalian glycoconjugates are illustrated and their chemical structures are advanced by the expression of the disaccharide units and code system; (2) the sizes and motifs of GalNAcα1 → specific lectin-glycan interactions are given and (3) the role of the polyvalent blood group A<sub>h</sub> and B<sub>h</sub> glycotopes as blood group AB antigens are proposed. These three highlights should provide an essential background required for the advances in this field.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":null,"pages":null},"PeriodicalIF":2.7000,"publicationDate":"2022-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Loci and motifs of the GalNAcα1 → 3/O related glycotopes in the mammalian glycoconjugates and their lectin recognition roles.\",\"authors\":\"Albert M Wu\",\"doi\":\"10.1007/s10719-022-10068-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Galα1 → and GalNAcα1 → are the two essential key sugars in human blood group AB active glycotopes, in which GalNAcα1 → related sequences are located at both sides of the nonreducing and the reducing ends of human blood group A active O-glycans. It is also found at the nonreducing ends of GlcNAc N-glycans and glycosphingolipid(GSL) of human blood group A active glycotopes (A<sub>h</sub>) and Forssman antigen (F<sub>p</sub>). When monosaccharides and their α, β anomers are involved in basic units to express the complex size of the combining sites of the GalNAcα1 → specific lectins, they can be divided into a cavity site to accommodate the GalNAcα → key sugar and a subsite with a wide and broad range of recognition area to adopt the rest part of sugar sequences or glycotopes. The function of the subsite is assumed to act as an enhancement factor to increase its affinity power. The following three points are the theme of this mini review: (1) the loci and distribution of the GalNAcα1 → related glycotopes in mammalian glycoconjugates are illustrated and their chemical structures are advanced by the expression of the disaccharide units and code system; (2) the sizes and motifs of GalNAcα1 → specific lectin-glycan interactions are given and (3) the role of the polyvalent blood group A<sub>h</sub> and B<sub>h</sub> glycotopes as blood group AB antigens are proposed. These three highlights should provide an essential background required for the advances in this field.</p>\",\"PeriodicalId\":12762,\"journal\":{\"name\":\"Glycoconjugate Journal\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2022-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Glycoconjugate Journal\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s10719-022-10068-6\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2022/8/13 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Glycoconjugate Journal","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s10719-022-10068-6","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2022/8/13 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 2
摘要
Galα1→和GalNAcα1→是人血AB型活性糖基中必不可少的两个关键糖,其中GalNAcα1→相关序列位于人血A型活性o型聚糖的非还原端和还原端两侧。它也存在于GlcNAc n -聚糖和人血A型活性糖基(Ah)和Forssman抗原(Fp)的鞘糖脂(GSL)的非还原端。当单糖及其α、β异构体参与基本单元表达GalNAcα1→特异性凝集素结合位点的复合体大小时,可分为容纳GalNAcα→关键糖的空腔位点和具有广泛识别区域以容纳其余糖序列或糖基的亚位点。假设子位点的功能是作为增强因子来增加其亲和力。本文主要从以下三个方面进行综述:(1)阐明哺乳动物糖缀合物中GalNAcα1→相关糖基的位点和分布,并通过双糖单元和编码系统的表达来确定其化学结构;(2)给出了GalNAcα1→特异性凝集素-聚糖相互作用的大小和基序;(3)提出了多价血型Ah和Bh糖基作为血型AB抗原的作用。这三个重点应该为这一领域的进展提供必要的背景。
Loci and motifs of the GalNAcα1 → 3/O related glycotopes in the mammalian glycoconjugates and their lectin recognition roles.
Galα1 → and GalNAcα1 → are the two essential key sugars in human blood group AB active glycotopes, in which GalNAcα1 → related sequences are located at both sides of the nonreducing and the reducing ends of human blood group A active O-glycans. It is also found at the nonreducing ends of GlcNAc N-glycans and glycosphingolipid(GSL) of human blood group A active glycotopes (Ah) and Forssman antigen (Fp). When monosaccharides and their α, β anomers are involved in basic units to express the complex size of the combining sites of the GalNAcα1 → specific lectins, they can be divided into a cavity site to accommodate the GalNAcα → key sugar and a subsite with a wide and broad range of recognition area to adopt the rest part of sugar sequences or glycotopes. The function of the subsite is assumed to act as an enhancement factor to increase its affinity power. The following three points are the theme of this mini review: (1) the loci and distribution of the GalNAcα1 → related glycotopes in mammalian glycoconjugates are illustrated and their chemical structures are advanced by the expression of the disaccharide units and code system; (2) the sizes and motifs of GalNAcα1 → specific lectin-glycan interactions are given and (3) the role of the polyvalent blood group Ah and Bh glycotopes as blood group AB antigens are proposed. These three highlights should provide an essential background required for the advances in this field.
期刊介绍:
Glycoconjugate Journal publishes articles and reviews on all areas concerned with:
function, composition, structure, biosynthesis, degradation, interactions, recognition and chemo-enzymatic synthesis of glycoconjugates (glycoproteins, glycolipids, oligosaccharides, polysaccharides and proteoglycans), biochemistry, molecular biology, biotechnology, immunology and cell biology of glycoconjugates, aspects related to disease processes (immunological, inflammatory, arthritic infections, metabolic disorders, malignancy, neurological disorders), structural and functional glycomics, glycoimmunology, glycovaccines, organic synthesis of glycoconjugates and the development of methodologies if biologically relevant, glycosylation changes in disease if focused on either the discovery of a novel disease marker or the improved understanding of some basic pathological mechanism, articles on the effects of toxicological agents (alcohol, tobacco, narcotics, environmental agents) on glycosylation, and the use of glycotherapeutics.
Glycoconjugate Journal is the official journal of the International Glycoconjugate Organization, which is responsible for organizing the biennial International Symposia on Glycoconjugates.