Further structural characterization of Echinococcus granulosus laminated layer carbohydrates: The blood-antigen P1-motif gives rise to branches at different points of the O-glycan chains.
Further structural characterization of Echinococcus granulosus laminated layer carbohydrates: The blood-antigen P1-motif gives rise to branches at different points of the O-glycan chains.
复制标题
细粒棘球蚴叠层碳水化合物的进一步结构表征：血抗原 P1 基序在 O-聚糖链的不同点产生分支。
DOI：
10.1093/glycob/cws220
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发表时间：
2013
期刊：
影响因子：
4.3
通讯作者：
Gerardo Lin
中科院分区：
文献类型：
--
作者：
浅海慎太郎;杉本幸子;松浪勝義;武田美雄;Gerardo Lin
绦虫是一类寄生扁虫，其糖生物学在很大程度上仍未被探索。细粒棘球绦虫是一种重要的寄生虫，其组织寄居幼虫阶段可引起包虫病。就是你。细粒幼虫通过大量的粘蛋白细胞外基质保护免受宿主的侵袭，这种细胞外基质被称为层状层(LL)。我们之前报道了(生物化学48：11678-11691)最丰富的L-O-多糖的分子结构，由多达六个单糖残基组成。这些是以核心1和核心2为基础的，在由Galpβ1-3残基链延伸的情况下，该链可以被Galpα1-4封顶。此外，核心2 GlcN可用Galpα1-4Galpβ1-4双糖修饰。检测到的较大的糖链还含有额外的HexNAc残基，这些残基不能用上述结构谱系解释。在这项工作中，我们通过质谱学(MS)和核磁共振(核磁共振)鉴定了六个额外的糖链。颗粒大小介于六到八个残基之间。它们的结构与已经描述的结构有关，但在含有GlcNAcpβ1-6或Galpα1-4Galpβ1-4GlcNAcpβ1-6的情况下，作为核心Galpβ1-3残基的分支。我们还获得了非核心Galpβ1-3残基可以类似地分支的证据。因此，新的基序与以前的信息一起可以解释MS在LL中检测到的所有多糖成分。此外，我们还发现抗棘球绦虫单抗E492(寄生虫免疫21：141,1999年)可以识别Galpα1-4Galpβ1-4GlcNAcp(血液P1抗原基序)。这解释了抗体与一系列棘球绦虫组织的反应性，因为P1基序也携带在该属的非LLN-聚糖和糖脂上。
The glycobiology of the cestodes, a class of parasitic flatworms, is still largely unexplored. An important cestode species isEchinococcus granulosus, the tissue-dwelling larval stage of which causes hydatid disease. TheE. granulosuslarva is protected from the host by a massive mucin-based extracellular matrix termed laminated layer (LL). We previously reported ( .Biochemistry48:11678–11691) the molecular structure of the most abundant LL O-glycans, comprising up to six monosaccharide residues. These are based on Cores 1 and 2, in cases elongated by a chain of Galpβ1-3 residues, which can be capped by Galpα1-4. In addition, the Core 2 GlcNAcpresidue can be decorated with the Galpα1-4Galpβ1-4 disaccharide. Larger glycans also detected contained additional HexNAc residues that could not be explained by the structural repertoire described above. In this work, we elucidate, by mass spectrometry (MS) and nuclear magnetic resonance (NMR), six additional glycans from theE. granulosusLL between six and eight residues in size. Their structures are related to those already described but in cases bear GlcNAcpβ1-6 or Galpα1-4Galpβ1-4GlcNAcpβ1-6 as ramifications on the core Galpβ1-3 residue. We also obtained evidence that noncore Galpβ1-3 residues can be similarly ramified. Thus, the new motif together with the previous information may explain all the glycan compositions detected in the LL by MS. In addition, we show that the anti-Echinococcusmonoclonal antibody E492 (Parasite Immunol21:141, 1999) recognizes Galpα1-4Galpβ1-4GlcNAcp(the blood P1-antigen motif). This explains the antibody's reactivity with a range ofEchinococcustissues, as the P1-motif is also carried on non-LL N-glycans and glycolipids from this genus.