A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments
文献类型：期刊论文
| 作者 | Wang, Yang1; Yuan, Wenjie1; Guo, Siqi2,3; Li, Qiqi1; Chen, Xiaomei1; Li, Cheng1; Liu, Qianying4; Sun, Lei4; Chen, Zhenguo4; Yuan, Zhenghong1 |
| 刊名 | NATURE COMMUNICATIONS
 |
| 出版日期 | 2022-08-08 |
| 卷号 | 13期号:1页码:4614 |
| DOI | 10.1038/s41467-022-32423-9 |
| 文献子类 | Article |
| 英文摘要 | Low solubility and stability of Escherichia coli produced single chain variable fragments (scFvs) restrict their applications. Here the authors report a 33-residue peptide tag which simultaneously increases the solubility and thermostability of multiple scFvs produced in Escherichia coli SHuffle strain. Single-chain variable fragments (scFvs), composed of variable domains of heavy and light chains of an antibody joined by a linker, share antigen binding capacity with their parental antibody. Due to intrinsically low solubility and stability, only two Escherichia coli-produced scFvs have been approved for therapy. Here we report that a 33-residue peptide, termed P17 tag, increases the solubility of multiple scFvs produced in Escherichia coli SHuffle strain by up to 11.6 fold. Hydrophilic sequence, especially charged residues, but not the predicted alpha-helical secondary structure of P17 tag, contribute to the solubility enhancement. Notably, the P17 tag elevates the thermostability of scFv as efficiently as intra-domain disulfide bonds. Moreover, a P17-tagged scFv targeting hepatitis B virus surface proteins shows over two-fold higher antigen-binding affinity and virus-neutralizing activity than the untagged version. These data strongly suggest a type I intramolecular chaperone-like activity of the P17 tag. Hence, the P17 tag could benefit the research, production, and application of scFv. |
| WOS关键词 | DISULFIDE BOND FORMATION ; HEPATITIS-B-VIRUS ; INTRAMOLECULAR CHAPERONE ; MONOCLONAL-ANTIBODIES ; PROTEIN EXPRESSION ; ACID ; HEPATOCYTES ; PATHWAY ; ENZYME ; DOMAIN |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| 出版者 | NATURE PORTFOLIO |
| WOS记录号 | WOS:000837856500013 |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/309312]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Chen, Shijie; Wang, Yong-Xiang |
| 作者单位 | 1.Fudan Univ, Shanghai Med Coll, Sch Basic Med Sci, Key Lab Med Mol Virol MOE NHC CAMS, Shanghai, Peoples R China; 2.Chinese Acad Sci, Drug Discovery & Design Ctr, Ctr Chem Biol, Shanghai Inst Mat Med,State Key Lab Drug Res, Shanghai, Peoples R China; 3.Nanchang Univ, Sch Pharm, Nanchang, Jiangxi, Peoples R China; 4.Fudan Univ, Inst Biomed Sci, Shanghai, Peoples R China; 5.UCAS, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou, Peoples R China; 6.Univ Hosp Freiburg, Dept Internal Med Mol Biol 2, Freiburg, Germany |
| 推荐引用方式 GB/T 7714 | Wang, Yang,Yuan, Wenjie,Guo, Siqi,et al. A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments[J]. NATURE COMMUNICATIONS,2022,13(1):4614. |
| APA | Wang, Yang.,Yuan, Wenjie.,Guo, Siqi.,Li, Qiqi.,Chen, Xiaomei.,...&Wang, Yong-Xiang.(2022).A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments.NATURE COMMUNICATIONS,13(1),4614. |
| MLA | Wang, Yang,et al."A 33-residue peptide tag increases solubility and stability of Escherichia coli produced single-chain antibody fragments".NATURE COMMUNICATIONS 13.1(2022):4614. |
入库方式： OAI收割
来源：上海药物研究所
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