DC Field | Value | Language |
---|---|---|
dc.contributor.author | Song, Shi-Jian | - |
dc.contributor.author | Diao, Hai-Ping | - |
dc.contributor.author | Moon, Byeongho | - |
dc.contributor.author | Yun, Areum | - |
dc.contributor.author | Hwang, Inhwan | - |
dc.date.accessioned | 2023-03-02T08:40:25Z | - |
dc.date.available | 2023-03-02T08:40:25Z | - |
dc.date.created | 2023-03-02 | - |
dc.date.issued | 2022-04 | - |
dc.identifier.issn | 1664-462X | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/116225 | - |
dc.description.abstract | <jats:p>Plants have long been considered a cost-effective platform for recombinant production. A recently recognized additional advantage includes the low risk of contamination of human pathogens, such as viruses and bacterial endotoxins. Indeed, a great advance has been made in developing plants as a “factory” to produce recombinant proteins to use for biopharmaceutical purposes. However, there is still a need to develop new tools for recombinant protein production in plants. In this study, we provide data showing that the B1 domain of Streptococcal protein G (GB1) can be a multi-functional domain of recombinant proteins in plants. N-terminal fusion of the GB1 domain increased the expression level of various target proteins ranging from 1.3- to 3.1-fold at the protein level depending on the target proteins. GB1 fusion led to the stabilization of the fusion proteins. Furthermore, the direct detection of GB1-fusion proteins by the secondary anti-IgG antibody eliminated the use of the primary antibody for western blot analysis. Based on these data, we propose that the small GB1 domain can be used as a versatile tag for recombinant protein production in plants.</jats:p> | - |
dc.language | English | - |
dc.publisher | Frontiers Media S.A. | - |
dc.relation.isPartOf | Frontiers in Plant Science | - |
dc.title | The B1 Domain of Streptococcal Protein G Serves as a Multi-Functional Tag for Recombinant Protein Production in Plants | - |
dc.type | Article | - |
dc.identifier.doi | 10.3389/fpls.2022.878677 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | Frontiers in Plant Science, v.13 | - |
dc.identifier.wosid | 000794055700001 | - |
dc.citation.title | Frontiers in Plant Science | - |
dc.citation.volume | 13 | - |
dc.contributor.affiliatedAuthor | Hwang, Inhwan | - |
dc.identifier.scopusid | 2-s2.0-85129584914 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | Y | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | HIGH-YIELD PRODUCTION | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordPlus | FUSION | - |
dc.subject.keywordPlus | THERAPEUTICS | - |
dc.subject.keywordPlus | CALNEXIN | - |
dc.subject.keywordPlus | MOLECULE | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordAuthor | plant-based molecular pharming | - |
dc.subject.keywordAuthor | Nicotiana benthamiana | - |
dc.subject.keywordAuthor | biopharmaceutical proteins | - |
dc.subject.keywordAuthor | GB1 | - |
dc.subject.keywordAuthor | protein folding | - |
dc.relation.journalWebOfScienceCategory | Plant Sciences | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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