Cited 0 times in Scipus Cited Count

The catalytic activity of a recombinant single chain variable fragment nucleic acid-hydrolysing antibody varies with fusion tag and expression host

DC Field Value Language
dc.contributor.authorLee, J-
dc.contributor.authorKim, M-
dc.contributor.authorSeo, Y-
dc.contributor.authorLee, Y-
dc.contributor.authorPark, H-
dc.contributor.authorByun, SJ-
dc.contributor.authorKwon, MH-
dc.date.accessioned2018-08-24T01:48:29Z-
dc.date.available2018-08-24T01:48:29Z-
dc.date.issued2017-
dc.identifier.issn0003-9861-
dc.identifier.urihttp://repository.ajou.ac.kr/handle/201003/15851-
dc.description.abstractThe antigen-binding properties of single chain Fv antibodies (scFvs) can vary depending on the position and type of fusion tag used, as well as the host cells used for expression. The issue is even more complicated with a catalytic scFv antibody that binds and hydrolyses a specific antigen. Herein, we investigated the antigen-binding and -hydrolysing activities of the catalytic anti-nucleic acid antibody 3D8 scFv expressed in Escherichia coli or HEK293f cells with or without additional amino acid residues at the N- and C-termini. DNA-binding activity was retained in all recombinant forms. However, the DNA-hydrolysing activity varied drastically between forms. The DNA-hydrolysing activity of E. coli-derived 3D8 scFvs was not affected by the presence of a C-terminal human influenza haemagglutinin (HA) or His tag. By contrast, the activity of HEK293f-derived 3D8 scFvs was completely lost when additional residues were included at the N-terminus and/or when a His tag was incorporated at the C-terminus, whereas a HA tag at the C-terminus did not diminish activity. Thus, we demonstrate that the antigen-binding and catalytic activities of a catalytic antibody can be separately affected by the presence of additional residues at the N- and C-termini, and by the host cell type.-
dc.language.isoen-
dc.subject.MESHAntibodies, Catalytic-
dc.subject.MESHCloning, Molecular-
dc.subject.MESHDNA-
dc.subject.MESHDNA Cleavage-
dc.subject.MESHEscherichia coli-
dc.subject.MESHGene Expression-
dc.subject.MESHHEK293 Cells-
dc.subject.MESHHemagglutinins-
dc.subject.MESHHistidine-
dc.subject.MESHHumans-
dc.subject.MESHKinetics-
dc.subject.MESHOligopeptides-
dc.subject.MESHPlasmids-
dc.subject.MESHProtein Binding-
dc.subject.MESHRecombinant Fusion Proteins-
dc.subject.MESHSequence Analysis, Protein-
dc.subject.MESHSingle-Chain Antibodies-
dc.titleThe catalytic activity of a recombinant single chain variable fragment nucleic acid-hydrolysing antibody varies with fusion tag and expression host-
dc.typeArticle-
dc.identifier.pmid28888872-
dc.contributor.affiliatedAuthor권, 명희-
dc.type.localJournal Papers-
dc.identifier.doi10.1016/j.abb.2017.09.004-
dc.citation.titleArchives of biochemistry and biophysics-
dc.citation.volume633-
dc.citation.date2017-
dc.citation.startPage110-
dc.citation.endPage117-
dc.identifier.bibliographicCitationArchives of biochemistry and biophysics, 633. : 110-117, 2017-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.identifier.eissn1096-0384-
dc.relation.journalidJ000039861-
Appears in Collections:
Journal Papers > School of Medicine / Graduate School of Medicine > Microbiology
Files in This Item:
There are no files associated with this item.

qrcode

해당 아이템을 이메일로 공유하기 원하시면 인증을 거치시기 바랍니다.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse