Abstract: Protein glycosylation greatly influences the structure, function, and pharmacokinetics of recombinant proteins. Here, growth media supplemented with metal ions is shown to modulate the protein glycosylation profile of recombinant proteins expressed in a variety of eukaryotic cell lines. In particular, millimolar amounts of ferric salts (e.g. ferric nitrate, ferric citrate, etc.) significantly increased the percentage of galactosylated N-glycan species. The effect on protein glycosylation was concentration-dependent manner up to 1.0 mM across multiple cell lines without adverse effects on cell viability. The use of iron supplements in cell culture media provides an efficient and effective approach towards the specific re-targeting of N-glycan glycoform profiles of recombinantly expressed proteins.

Abstract: Protein glycosylation greatly influences the structure, function, and pharmacokinetics of recombinant proteins. Here, growth media supplemented with metal ions is shown to modulate the protein glycosylation profile of recombinant proteins expressed in a variety of eukaryotic cell lines. In particular, millimolar amounts of ferric salts (e.g. ferric nitrate, ferric citrate, etc.) significantly increased the percentage of galactosylated N-glycan species. The effect on protein glycosylation was concentration-dependent manner up to 1.0 mM across multiple cell lines without adverse effects on cell viability. The use of iron supplements in cell culture media provides an efficient and effective approach towards the specific re-targeting of N-glycan glycoform profiles of recombinantly expressed proteins.

Abstract: Protein glycosylation greatly influences the structure, function, and pharmacokinetics of recombinant proteins. Here, growth media supplemented with metal ions is shown to modulate the protein glycosylation profile of recombinant proteins expressed in a variety of eukaryotic cell lines. In particular, millimolar amounts of ferric salts (e.g. ferric nitrate, ferric citrate, etc.) significantly increased the percentage of galactosylated N-glycan species. The effect on protein glycosylation was concentration-dependent manner up to 1.0 mM across multiple cell lines without adverse effects on cell viability. The use of iron supplements in cell culture media provides an efficient and effective approach towards the specific re-targeting of N-glycan glycoform profiles of recombinantly expressed proteins.

Abstract: A method of enhancing heterologous protein secretion in a yeast cell is disclosed. In one embodiment, the method comprising the steps of engineering a yeast cell to overexpress at last one gene selected from the group consisting of CCW12, CWP2, SED1, RPP0, ERO1 and their homologs, supplying the yeast cell with a nucleic acid encoding a heterologous protein and obtaining increased expression of the heterologous protein, wherein the expression is increased relative to the protein expression in a yeast cell that does not overexpress a gene selected from the group consisting of CCW12, CWP2, SED1, RPP0, ERO1 and their homologs.

Abstract: A method of enhancing heterologous protein secretion in a yeast cell is disclosed. In one embodiment, the method comprising the steps of engineering a yeast cell to overexpress at last one gene selected from the group consisting of CCW12, CWP2, SED1, RPP0, ERO1 and their homologs, supplying the yeast cell with a nucleic acid encoding a heterologous protein and obtaining increased expression of the heterologous protein, wherein the expression is increased relative to the protein expression in a yeast cell that does not overexpress a gene selected from the group consisting of CCW12, CWP2, SED1, RPP0, ERO1 and their homologs.