Learning Centre

Following nature's roadmap

 |  Login

Show simple item record

dc.contributor Aalto-yliopisto fi
dc.contributor Aalto University en
dc.contributor.author Koskela, Essi V.
dc.contributor.author de Ruijter, Jorg C.
dc.contributor.author Frey, Alexander D.
dc.date.accessioned 2019-05-06T09:12:18Z
dc.date.available 2019-05-06T09:12:18Z
dc.date.issued 2017-08-01
dc.identifier.citation Koskela , E V , de Ruijter , J C & Frey , A D 2017 , ' Following nature's roadmap : folding factors from plasma cells led to improvements in antibody secretion in S. cerevisiae ' , BIOTECHNOLOGY JOURNAL , vol. 12 , no. 8 , 1600631 . https://doi.org/10.1002/biot.201600631 en
dc.identifier.issn 1860-6768
dc.identifier.other PURE UUID: 5acf6a1e-68fe-44a5-88e8-d32e7e72d9bd
dc.identifier.other PURE ITEMURL: https://research.aalto.fi/en/publications/following-natures-roadmap(5acf6a1e-68fe-44a5-88e8-d32e7e72d9bd).html
dc.identifier.other PURE LINK: http://www.scopus.com/inward/record.url?scp=85019898032&partnerID=8YFLogxK
dc.identifier.other PURE FILEURL: https://research.aalto.fi/files/32914199/CHEM_Koskela_etal_Following_nature_roadmap_2017_Biotech_journal.pdf
dc.identifier.uri https://aaltodoc.aalto.fi/handle/123456789/37670
dc.description.abstract Therapeutic protein production in yeast is a reality in industry with an untapped potential to expand to more complex proteins, such as full-length antibodies. Despite numerous engineering approaches, cellular limitations are preventing the use of Saccharomyces cerevisiae as the titers of recombinant antibodies are currently not competitive. Instead of a host specific approach, the possibility of adopting the features from native producers of antibodies, plasma cells, to improve antibody production in yeast. A subset of mammalian folding factors upregulated in plasma cells for expression in yeast and screened for beneficial effects on antibody secretion using a high-throughput ELISA platform was selected. Co-expression of the mammalian chaperone BiP, the co-chaperone GRP170, or the peptidyl-prolyl isomerase FKBP2, with the antibody improved specific product yields up to two-fold. By comparing strains expressing FKBP2 or the yeast PPIase Cpr5p, the authors demonstrate that speeding up peptidyl-prolyl isomerization by upregulation of catalyzing enzymes is a key factor to improve antibody titers in yeast. The findings show that following the route of plasma cells can improve product titers and contribute to developing an alternative yeast-based antibody factory. en
dc.format.extent 11
dc.format.mimetype application/pdf
dc.language.iso en en
dc.publisher Wiley-VCH Verlag
dc.relation.ispartofseries BIOTECHNOLOGY JOURNAL en
dc.relation.ispartofseries Volume 12, issue 8 en
dc.rights openAccess en
dc.subject.other Applied Microbiology and Biotechnology en
dc.subject.other Molecular Medicine en
dc.subject.other 1182 Biochemistry, cell and molecular biology en
dc.title Following nature's roadmap en
dc.type A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä fi
dc.description.version Peer reviewed en
dc.contributor.department Department of Bioproducts and Biosystems
dc.subject.keyword Antibodies
dc.subject.keyword Protein folding
dc.subject.keyword Synthetic biology
dc.subject.keyword Yeast
dc.subject.keyword Applied Microbiology and Biotechnology
dc.subject.keyword Molecular Medicine
dc.subject.keyword 1182 Biochemistry, cell and molecular biology
dc.identifier.urn URN:NBN:fi:aalto-201905062790
dc.identifier.doi 10.1002/biot.201600631
dc.type.version acceptedVersion

Files in this item

Files Size Format View

There are no open access files associated with this item.

This item appears in the following Collection(s)

Show simple item record

Search archive

Advanced Search

article-iconSubmit a publication