Abstract: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the Fc?RI, Fc?RIIA, and Fc?RIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity.

Abstract: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the Fc?RI, Fc?RIIA, and Fc?RIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity.

Abstract: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the Fc?RI, Fc?RIIA, and Fc?RIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity.

Abstract: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the Fc?RI, Fc?RIIA, and Fc?RIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity.

Abstract: Antibody and other Fc-containing molecules with glycosylation variations in the Fc region show increased resistance to proteases, such as pepsin, plasmin, trypsin, chymotrypsin, a matrix metalloproteinase, a serine endopeptidase, and a cysteine protease. The Fc-containing molecules are useful in the treatment of various diseases and disorders.

Abstract: Antibody preparations with substantially homogeneous and unsialylated glycoforms, such as G0 and G2, are prepared by enzymatic treatment, expression under certain conditions, use of particular host cells, and contact with serum. These antibody preparations resist cleavage by proteases, such as papain, ficin, bromolein, pepsin, a matrix metalloproteinase, such as MMP-7, neutrophil elastase (HNE), stromelysin (MMP-3) and macrophage elastase (MMP-12), and glycosylation modification enzymes. The antibody preparations with substantially homogeneous and unsialylated glycoforms and methods of testing for glycosylation in an antibody are useful in connection with characterization of antibody properties and/or in diseases or conditions characterized by an increase in protease activity.

Abstract: Antibody preparations with reduced hydrophobic interactions between Fc side chains and sugar residues of the oligosaccharide backbone present in the CH2 regions of the Fc and/or increased hydrophilic reactions between Fc side chains and sugar residues in the CH2 regions of the Fc-containing protein compared to a wild-type antibody, are prepared by enzymatic treatment, expression under certain conditions, use of particular host cells, and contact with serum. These antibody preparations resist cleavage by proteases, such as papain, ficin, bromolein, pepsin, a matrix metalloproteinase, such as MMP-7, neutrophil elastase (HNE), stromelysin (MMP-3) and macrophage elastase (MMP-12), and glycosylation modification enzymes.

Abstract: An enzymatic method for synthesizing oligosaccharides comprising a terminal Gal-alpha(1,3)-Gal-beta(1-4)GlcNac is used to produce Fc-containing molecules with certain properties. The methods modify glycoproteins that interact with receptors or are processed in vivo and recognized as unique epitopes. In particular, the glycan groups on a therapeutic antibody capable of interaction with Fc-receptors are modified.

Abstract: The properties of an Fc-containing protein, for example, an antibody, are controlled by altering the sialylation of the oligosaccharides in the Fc region by transfecting the cell line expressing the Fc-containing protein with a vector sequence encoding a sialidase. The modified Fc-containing proteins have therapeutic utility in diseases or conditions in which it is desirable to control the affinity for one or more of the Fc?RI, Fc?RIIA, and Fc?RIIIA receptors, ADCC activity, macrophage or monocyte activation, serum half-life, and avidity.

Abstract: This invention relates to novel glycoprotein glycoform preparations comprising the substantially homogenous glycoprotein glycoforms. More particularly the invention relates to substantially homogenous glycoprotein preparations comprising a particular Fc glycan and methods for producing, detecting, enriching and purifying the glycoforms. The invention further relates to immunoglobulins and especially antibodies comprising a CH2 domain having a particular glycan. Provided are compositions including pharmaceutical compositions methods of using the preparations as well as articles of manufacture comprising the preparations.

Abstract: This invention relates to novel glycoprotein glycoform preparations comprising the substantially homogeneous glycoprotein glycoforms and combinations thereof. More particularly the invention relates to glycoprotein preparations comprising a particular Fc glycoforms and methods for producing, detecting, enriching and purifying the glycoforms. The invention further relates to immunoglobulins and especially antibodies comprising a CH2 domain having particular N-linked glycans. Provided are compositions including pharmaceutical compositions methods of using the preparations as well as articles of manufacture comprising the preparations.