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dc.contributor.authorFinnis, CJA-
dc.contributor.authorPayne, T-
dc.contributor.authorHay, J-
dc.contributor.authorDodsworth, N-
dc.contributor.authorWilkinson, D-
dc.contributor.authorMorton, P-
dc.contributor.authorSaxton, MJ-
dc.contributor.authorTooth, DJ-
dc.contributor.authorEvans, RW-
dc.contributor.authorGoldenberg, H-
dc.contributor.authorScheiber-Mojdehkar, B-
dc.contributor.authorTernes, N-
dc.contributor.authorSleep, D-
dc.identifier.citationMicrobial Cell Factories, 9:87 (17 November 2010)en_US
dc.descriptionThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.en_US
dc.description.abstractBackground: Animal-free recombinant proteins provide a safe and effective alternative to tissue or serum-derived products for both therapeutic and biomanufacturing applications. While recombinant insulin and albumin already exist to replace their human counterparts in cell culture media, until recently there has been no equivalent for serum transferrin.Results: The first microbial system for the high-level secretion of a recombinant transferrin (rTf) has been developed from Saccharomyces cerevisiae strains originally engineered for the commercial production of recombinant human albumin (Novozymes' Recombumin® USP-NF) and albumin fusion proteins (Novozymes' albufuse®). A full-length non-N-linked glycosylated rTf was secreted at levels around ten-fold higher than from commonly used laboratory strains. Modification of the yeast 2 μm-based expression vector to allow overexpression of the ER chaperone, protein disulphide isomerase, further increased the secretion of rTf approximately twelve-fold in high cell density fermentation. The rTf produced was functionally equivalent to plasma-derived transferrin.Conclusions: A Saccharomyces cerevisiae expression system has enabled the cGMP manufacture of an animal-free rTf for industrial cell culture application without the risk of prion and viral contamination, and provides a high-quality platform for the development of transferrin-based therapeutics.en_US
dc.subjectanimal-free recombinant proteinsen_US
dc.subjectSaccharomyces cerevisiaeen_US
dc.subjectrecombinant transferrinen_US
dc.subjectN-linked glycosylation sitesen_US
dc.titleHigh-level production of animal-free recombinant transferrin from Saccharomyces cerevisiaeen_US
dc.relation.isPartOfMicrobial Cell Factories-
dc.relation.isPartOfMicrobial Cell Factories-
Appears in Collections:Dept of Life Sciences Research Papers

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