{"title":"Analysis of <i>N</i>-glycan profile of Arabidopsis <i>alg3</i> cell culture.","authors":"Ratna Sariyatun, Hiroyuki Kajiura, Juthamard Limkul, Ryo Misaki, Kazuhito Fujiyama","doi":"10.5511/plantbiotechnology.21.1025a","DOIUrl":null,"url":null,"abstract":"<p><p><i>N</i>-Glycosylation is essential for protein stability, activity and characteristics, and is often needed to deliver pharmaceutical glycoproteins to target cells. A paucimannosidic structure, Man<sub>3</sub>GlcNAc<sub>2</sub> (M3), has been reported to enable cellular uptake of glycoproteins through the mannose receptor (MR) in humans, and such uptake has been exploited for the treatment of certain diseases. However, M3 is generally produced at a very low level in plants. In this study, a cell culture was established from an Arabidopsis <i>alg3</i> mutant plant lacking asparagine-linked glycosylation 3 (ALG3) enzyme activity. Arabidopsis <i>alg3</i> cell culture produced glycoproteins with predominantly M3 and GlcNAc-terminal structures, while the amount of plant-specific <i>N</i>-glycans was very low. Pharmaceutical glycoproteins with these characteristics would be valuable for cellular delivery through the MR, and safe for human therapy.</p>","PeriodicalId":1,"journal":{"name":"Accounts of Chemical Research","volume":null,"pages":null},"PeriodicalIF":16.4000,"publicationDate":"2021-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8761587/pdf/plantbiotechnology-38-4-21.1025a.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Accounts of Chemical Research","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.5511/plantbiotechnology.21.1025a","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
N-Glycosylation is essential for protein stability, activity and characteristics, and is often needed to deliver pharmaceutical glycoproteins to target cells. A paucimannosidic structure, Man3GlcNAc2 (M3), has been reported to enable cellular uptake of glycoproteins through the mannose receptor (MR) in humans, and such uptake has been exploited for the treatment of certain diseases. However, M3 is generally produced at a very low level in plants. In this study, a cell culture was established from an Arabidopsis alg3 mutant plant lacking asparagine-linked glycosylation 3 (ALG3) enzyme activity. Arabidopsis alg3 cell culture produced glycoproteins with predominantly M3 and GlcNAc-terminal structures, while the amount of plant-specific N-glycans was very low. Pharmaceutical glycoproteins with these characteristics would be valuable for cellular delivery through the MR, and safe for human therapy.
n -糖基化对蛋白质的稳定性、活性和特性至关重要,并且通常需要将药用糖蛋白递送到靶细胞。据报道,一种低甘露糖苷结构,Man3GlcNAc2 (M3),可以通过人体甘露糖受体(MR)使细胞摄取糖蛋白,并且这种摄取已被用于治疗某些疾病。然而,工厂通常产生的M3水平很低。在这项研究中,建立了一个缺乏天冬酰胺连接糖基化3 (alg3)酶活性的拟南芥alg3突变体的细胞培养。拟南芥alg3细胞培养产生的糖蛋白以M3和glcnac末端结构为主,而植物特异性n -聚糖的含量很低。具有这些特征的药用糖蛋白对于通过核磁共振的细胞递送是有价值的,并且对人类治疗是安全的。
期刊介绍:
Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance.
Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.