Abstract: The present application relates to the field of glyco-engineering, more specifically to glyco-engineering of Fc-containing molecules, such as antibodies. It is shown herein that Fc-containing molecules with a specific glycosylation pattern have a considerably longer circulating half-life in vivo, without having an altered binding affinity for their respective antigen. This has therapeutic implications in reducing the frequency with which these molecules need to be administered, without affecting therapeutic efficacy. Also, cells are provided that can produce the Fc molecules with the desired glycosylation pattern.

Abstract: The present application relates to the field of glyco-engineering and, more specifically, to eukaryotic cells wherein both an endoglucosaminidase is present and made deficient in UDP-galactose 4-epimerase (GalE). Typically, a glycoprotein is also present in the cells. These cells can be used to deglycosylate or partly deglycosylate the (exogenous) glycoprotein, in particular, without the need for adding an extra enzyme. Methods are also provided for the application of these cells in protein production.

Abstract: The present application provides glycosylation engineered higher eukaryotic cells which produce homogeneous forms of sialylated glycans present on a recombinant glycoprotein. In particular, the glycosylation engineered higher eukaryotic cells produce homogeneous forms of small N-glycan structures which carry terminal sialic acid residues. In addition, the invention provides glycan-conjugates based on specific coupling with sialic acid residues present on the recombinant glycoproteins.

Abstract: The present invention provides means and methods for the production in eukaryotic cells of homogeneous forms of small glycan structures which carry terminal galactose residues. In addition, the invention provides glycan-conjugates based on specific coupling with galactose residues present on the recombinant glycoproteins.

Abstract: The present application relates to the field of glyco-engineering, more specifically to glyco-engineering of Fc-containing molecules, such as antibodies. It is shown herein that Fc-containing molecules with a specific glycosylation pattern have a considerably longer circulating half-life in vivo, without having an altered binding affinity for their respective antigen. This has therapeutic implications in reducing the frequency with which these molecules need to be administered, without affecting therapeutic efficacy. Also, cells are provided that can produce the Fc molecules with the desired glycosylation pattern.

Abstract: The present application relates to the field of glyco-engineering, more specifically to glyco-engineering of Fc-containing molecules, such as antibodies. It is shown herein that Fc-containing molecules with a specific glycosylation pattern have a considerably longer circulating half-life in vivo, without having an altered binding affinity for their respective antigen. This has therapeutic implications in reducing the frequency with which these molecules need to be administered, without affecting therapeutic efficacy. Also, cells are provided that can produce the Fc molecules with the desired glycosylation pattern.

Abstract: The present application relates to the field of glyco-engineering and, more specifically, to eukaryotic cells wherein both an endoglucosaminidase is present and made deficient in UDP-galactose 4-epimerase (GalE). Typically, a glycoprotein is also present in the cells. These cells can be used to deglycosylate or partly deglycosylate the (exogenous) glycoprotein, in particular, without the need for adding an extra enzyme. Methods are also provided for the application of these cells in protein production.

Abstract: The present application relates to the field of glyco-engineering, more specifically to glyco-engineering of Fc-containing molecules, such as antibodies. It is shown herein that Fc-containing molecules with a specific glycosylation pattern have a considerably longer circulating half-life in vivo, without having an altered binding affinity for their respective antigen. This has therapeutic implications in reducing the frequency with which these molecules need to be administered, without affecting therapeutic efficacy. Also, cells are provided that can produce the Fc molecules with the desired glycosylation pattern.