DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chung, Jae-Hee | ko |
dc.contributor.author | Hong, Seon-Hui | ko |
dc.contributor.author | Seo, Nari | ko |
dc.contributor.author | Kim, Tae-Shin | ko |
dc.contributor.author | An, Hyun Joo | ko |
dc.contributor.author | Lee, Pedro | ko |
dc.contributor.author | Shin, Eui-Cheol | ko |
dc.contributor.author | Kim, Ho Min | ko |
dc.date.accessioned | 2019-12-30T08:20:07Z | - |
dc.date.available | 2019-12-30T08:20:07Z | - |
dc.date.created | 2019-12-30 | - |
dc.date.created | 2019-12-30 | - |
dc.date.created | 2019-12-30 | - |
dc.date.issued | 2020-01 | - |
dc.identifier.citation | CYTOKINE, v.125 | - |
dc.identifier.issn | 1043-4666 | - |
dc.identifier.uri | http://hdl.handle.net/10203/270726 | - |
dc.description.abstract | Interferon lambda 4 (IFN lambda 4) has been recently known and studied for its role in hepatitis C virus (HCV) infection, but its clinical potential is significantly hampered due to its poor expression in vitro. Our study reports the successful production of IFN lambda 4 from a mammalian cell line through a glycoengineering and structure-based approach. We introduced de novo N-glycosylation of IFN lambda 4, guided by structural analysis, and produced IFN lambda 4 variants in Expi293F that displayed improved expression and potency. To preserve the structure and functionality of IFN lambda 4, the model structure of the IFN lambda 4 signaling complex was analyzed and the N-glycosylation candidate sites were selected. The receptor binding activity of engineered IFN lambda 4 variants and their receptor-mediated signaling pathway were similar to the E. coli version of IFNM (eIFN lambda 4), while the antiviral activity and induction levels of interferon-stimulated gene (ISG) were all more robust in our variants. Our engineered IFN lambda 4 variants may be further developed for clinical applications and utilized in basic research to decipher the immunological roles of IFN lambda 4. | - |
dc.language | English | - |
dc.publisher | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | - |
dc.title | Structure-based glycoengineering of interferon lambda 4 enhances its productivity and anti-viral potency | - |
dc.type | Article | - |
dc.identifier.wosid | 000501391800028 | - |
dc.identifier.scopusid | 2-s2.0-85071520627 | - |
dc.type.rims | ART | - |
dc.citation.volume | 125 | - |
dc.citation.publicationname | CYTOKINE | - |
dc.identifier.doi | 10.1016/j.cyto.2019.154833 | - |
dc.contributor.localauthor | Shin, Eui-Cheol | - |
dc.contributor.localauthor | Kim, Ho Min | - |
dc.contributor.nonIdAuthor | Seo, Nari | - |
dc.contributor.nonIdAuthor | An, Hyun Joo | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | IFN lambda 4 | - |
dc.subject.keywordAuthor | Glycoengineering | - |
dc.subject.keywordAuthor | Homology modeling | - |
dc.subject.keywordAuthor | Type III interferon signaling | - |
dc.subject.keywordAuthor | Anti-viral activity | - |
dc.subject.keywordPlus | IFN | - |
dc.subject.keywordPlus | GLYCOSYLATION | - |
dc.subject.keywordPlus | RECEPTOR | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | ALPHA | - |
dc.subject.keywordPlus | HCV | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | CLEARANCE | - |
dc.subject.keywordPlus | SECRETION | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.