Patent classifications
C12Y302/01096
METHOD
The invention relates to a method for improving the benefit of a therapy or a therapeutic agent to a subject. The method comprises administering to the subject an agent which reduces Fc receptor binding of serum IgG molecules in the subject; and subsequently administering said therapy or said therapeutic agent to the subject. The invention also relates to a method for reducing the effect of pathogenic autoantibodies in a subject, the method comprising (a) administering to the subject an agent which reduces Fc receptor binding of serum IgG molecules in the subject and optionally (b) subsequently subjecting the subject to a treatment which removes endogenous autoantibodies. The invention also relates to a kit for carrying out a method of the invention.
Means and Methods for Generating Complex Glycans Derived From Fungal Engineered Hosts
The present application relates to the field of glyco-engineering, more specifically to glycosylation-engineered fungal cells, more specifically glycosylation-engineered yeast cells, optimized to produce highly homogenous forms of complex N-glycans on recombinant proteins. The invention specifically relates to methods to obtain pharmaceutical compositions comprising recombinant glycoproteins which have homogenous forms of complex N-glycans. In addition, the invention relates to novel pharmaceutical compositions which result from the methods of the invention.
ENDO-S2 MUTANTS AS GLYCOSYNTHASES, METHOD OF MAKING AND USE FOR GLYCOENGINEERING OF GLYCOPROTEINS
The present invention provides for recombinant Endo-S2 mutants (named Endo-S2 glycosynthases) that exhibit reduced hydrolysis activity and increased transglycosylation activity for the synthesis of glycoproteins wherein a desired sugar chain is added to a fucosylated or nonfucosylated GlcNAc-IgG acceptor. As such, the present invention allows for the synthesis and remodeling of therapeutic antibodies thereby providing for certain biological activities, such as, prolonged half-life time in vivo, less immunogenicity, enhanced in vivo activity, increased targeting ability, and/or ability to deliver a therapeutic agent.
IN VIVO POST-TRANSLATIONAL PROCESSING OF TARGET PROTEIN BY FURIN IN PLANTS: ENGINEERING, EXPRESSION AND PRODUCTION OF FUNCTIONAL ACTIVE HUMAN FURIN IN N. BENTHAMIANA PLANTS
Materials and methods of in vivo possessing of target proteins in plants by co-expressing with proprotein processing enzyme, human Furin, are provided. A method of expressing highly soluble and functional active human Furin in plants also is provided.
Cells producing glycoproteins having altered glycosylation patterns and method and use thereof
The disclosure relates to the field of glyco-engineering, more specifically, to eukaryotic cells wherein both an endoglucosaminidase and a glycoprotein are present. 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. According to one specific aspect, the eukaryotic cells are glyco-engineered yeast cells in which, additionally, at least one exogenous enzyme needed for complex glycosylation is present, e.g., allowing easier separation of differentially glycosylated glycoproteins.
COMBINED THERAPEUTIC USE OF ANTIBODIES AND IMMUNOGLOBULIN G-DEGRADING ENZYMES
The invention relates to compositions comprising therapeutic antibodies, and uses and methods for increasing the potency of therapeutic antibodies. In particular, the invention provides a composition comprising (i) an agent which reduces Fc receptor binding of endogenous serum antibodies, and (ii) a therapeutic antibody, preferably a therapeutic antibody which is resistant to the agent. The therapeutic antibody may be administered to the subject after a set time interval, or the blood of the subject may be treated with the agent prior to administration of the therapeutic antibody.
Enzymes and methods for cleaving n-glycans from glycoproteins
Provided herein are deglycosylating enzymes that remove a broad range of N-glycans from N-glycosylated proteins. Further provided are methods of recombinantly producing and expressing the deglycosylating enzymes. The presently described deglycosylating enzymes can be used to produce free glycans for characterization, and for prebiotic and immunostimulatory uses. In addition, the presently described deglycosylating enzymes can be used to produce deglycosylated proteins for characterization, to improve digestion, and to reduce immunogenicity.
Endo-S2 mutants as glycosynthases, method of making and use for glycoengineering of glycoproteins
The present invention provides for recombinant Endo-S2 mutants (named Endo-S2 glycosynthases) that exhibit reduced hydrolysis activity and increased transglycosylation activity for the synthesis of glycoproteins wherein a desired sugar chain is added to a fucosylated or nonfucosylated GlcNAc-IgG acceptor. As such, the present invention allows for the synthesis and remodeling of therapeutic antibodies thereby providing for certain biological activities, such as, prolonged half-life time in vivo, less immunogenicity, enhanced in vivo activity, increased targeting ability, and/or ability to deliver a therapeutic agent.
Endo-S2 mutants as glycosynthases, method of making and use for glycoengineering of glycoproteins
The present invention provides for recombinant Endo-S2 mutants (named Endo-S2 glycosynthases) that exhibit reduced hydrolysis activity and increased transglycosylation activity for the synthesis of glycoproteins wherein a desired sugar chain is added to a fucosylated or nonfucosylated GlcNAc-IgG acceptor. As such, the present invention allows for the synthesis and remodeling of therapeutic antibodies thereby providing for certain biological activities, such as, prolonged half-life time in vivo, less immunogenicity, enhanced in vivo activity, increased targeting ability, and/or ability to deliver a therapeutic agent.
Endos mutant enzyme
The present invention provides an EndoS mutant enzyme having an amino acid sequence of EndoS D233Q and further having a particular additional mutation and exhibiting a reduced hydrolysis activity, in comparison with the activity of EndoS D233Q, to an N-linked sugar chain (N297-linked sugar chain) linked to Asn at position 297 in IgG and a gene encoding the same.