Grafting glycoprotein-derived oligosaccharides structures onto non-glycosylated polypeptides.

microPublication biology Pub Date : 2024-10-30 eCollection Date: 2024-01-01 DOI:10.17912/micropub.biology.001314
Danya Medina-Carrasco, Lisandra García de Castro Cuspineda, Luis Gabriel González-Lodeiro, Satomy Pousa, Miladys Limonta, Vivian Huerta Galindo
{"title":"Grafting glycoprotein-derived oligosaccharides structures onto non-glycosylated polypeptides.","authors":"Danya Medina-Carrasco, Lisandra García de Castro Cuspineda, Luis Gabriel González-Lodeiro, Satomy Pousa, Miladys Limonta, Vivian Huerta Galindo","doi":"10.17912/micropub.biology.001314","DOIUrl":null,"url":null,"abstract":"<p><p>Properties of recombinant glycoproteins can be altered by the addition of oligosaccharide structures specific to the cells used for its heterologous expression. A methodology was implemented to obtain a glycopeptide preparation useful to elucidate the role of carbohydrates in the immunogenicity and antigenicity of glycoproteins. It consists on the digestion of the protein, followed by selective capture of the oligosaccharides bound to di-/tripeptides, and their grafting onto a non-glycosylated receptor protein by chemical crosslinking. Glycopeptides derived from C-RBD-H6 PP protein, the active ingredient of the Abdala vaccine were efficiently grafted onto a non-glycosylated protein as evidenced by western blotting.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-10-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11561553/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001314","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Properties of recombinant glycoproteins can be altered by the addition of oligosaccharide structures specific to the cells used for its heterologous expression. A methodology was implemented to obtain a glycopeptide preparation useful to elucidate the role of carbohydrates in the immunogenicity and antigenicity of glycoproteins. It consists on the digestion of the protein, followed by selective capture of the oligosaccharides bound to di-/tripeptides, and their grafting onto a non-glycosylated receptor protein by chemical crosslinking. Glycopeptides derived from C-RBD-H6 PP protein, the active ingredient of the Abdala vaccine were efficiently grafted onto a non-glycosylated protein as evidenced by western blotting.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
将糖蛋白衍生的寡糖结构嫁接到非糖基化多肽上。
重组糖蛋白的特性可通过添加用于异源表达的细胞所特有的寡糖结构而改变。我们采用了一种方法来获得糖肽制剂,这种方法有助于阐明碳水化合物在糖蛋白的免疫原性和抗原性中的作用。该方法包括消化蛋白质,然后选择性地捕获与二肽/三肽结合的寡糖,并通过化学交联将其接枝到非糖基化受体蛋白上。从 C-RBD-H6 PP 蛋白(Abdala 疫苗的有效成分)中提取的糖肽有效地接枝到了非糖基化蛋白上,这一点已通过 Western 印迹得到证明。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
审稿时长
3 weeks
期刊最新文献
Erratum: Corrigendum: tRNA Arg binds in vitro TDP-43 RNA recognition motifs and ligand of Ate1 protein LIAT1. Two K2P Channels, TWK-46 and TWK-26 do not affect C. elegans Egg-Laying Behavior. Wild-Type Drosophila melanogaster Strains Respond Differentially to Rotenone Exposure. Molecular evidence supports the functionality of a protein-trapped endogenous allele of Dally-like protein. Heat Stress, Starvation, and Heat Stress Plus Starvation Cause Unique Transcriptomic Responses in the Economically Important Red Abalone Haliotis rufescens.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1