Patent classifications
C12Y302/01051
Compositions and methods for producing polypeptides with a modified glycosylation pattern in plant cells
A method of modifying a glycosylation pattern of a polypeptide-of-interest in a plant or plant cell is provided. The method comprising expressing in a plant or plant cell transformed to express at least one glycosidase in a subcellular compartment, a nucleic acid sequence encoding the polypeptide-of-interest, such that the at least one glycosidase and the polypeptide-of-interest are co-localized to the subcellular compartment of the plant or plant cell, thereby modifying the glycosylation pattern of the polypeptide-of-interest in the plant or plant cell.
PROTEASE COMPOSITIONS FOR USE IN MODIFYING SEMEN
Provided herein are edible compositions for reducing semen viscosity and/or enhancing semen flavor, and methods of using and preparing such compositions.
COMPOSITIONS AND METHODS FOR PRODUCING POLYPEPTIDES WITH A MODIFIED GLYCOSYLATION PATTERN IN PLANT CELLS
The A method of modifying a glycosylation pattern of a polypeptide-of-interest in a plant or plant cell is provided. The method comprising expressing in a plant or plant cell transformed to express at least one glycosidase in a subcellular compartment, a nucleic acid sequence encoding the polypeptide-of-interest, such that the at least one glycosidase and the polypeptide-of-interest are co-localized to the subcellular compartment of the plant or plant cell, thereby modifying the glycosylation pattern of the polypeptide-of-interest in the plant or plant cell.
Cellulose and/or hemicelluloses degrading enzymes from Macrophomina phaseolina and uses thereof
The present invention provides nucleotide sequences of Macrophomina phaseolina (“M. phaseolina”) that encodes proteins/enzymes with cellulolytic activity, including a cellulase activity, a endoglucanase, a cellobiohydrolase, a β-glucosidase, a a-glucosidase, a xylanase, a mannanse, a β-xylosidase, a a-xylosidase, a galactosidase, an arabinofuranosidase, a a-fucosidases, a β-galactanase, an unsaturated β-glucuronyl hydrolase and/or oligomerase activity. Vectors, expression constructs and host cells comprising and/or consisting of the nucleotide sequences of the enzyme genes are also provided. The invention further provides methods for producing the enzymes and methods for modifying the enzymes in order to improve their desirable characteristics. The enzymes of the invention can be used in a variety of, but not limited to, pharmaceutical, agricultural, food and feed processing, biofuel, energy efficiency and industrial contexts. These enzymes are also useful for complete hydrolysis of lignocellulosic biomass into simple sugar that can then be fermented to liquid fuels and chemical feedstocks.
Anti-TNF-alpha glycoantibodies and uses thereof
The present disclosure relates to a novel class of anti-TNFα monoclonal antibodies or antigen binding fragments comprising a homogeneous population of anti-TNFα IgG molecules having the same N-glycan on each of Fc. The antibodies of the invention can be produced from anti-TNFα monoclonal antibodies by Fc glycoengineering. The glycoantibodies of the invention may have improved therapeutic values compared to the corresponding monoclonal antibodies that have not been glycoengineered.
Fucosidase from bacteroides and methods using the same
The present disclosure relates to an α-fucosidase having α-(1,2), α-(1,3), α-(1,4), and α-(1,6) fucosidase activity. The present disclosure also relates to the compositions comprising the α-fucosidase, and the methods of producing and using the α-fucosidase in cleaving α-(1,2), α-(1,3), α-(1,4), and/or α-(1,6)-linked fucoses in the glycoconjugates.
COMPOSITIONS AND METHODS FOR PRODUCING POLYPEPTIDES WITH A MODIFIED GLYCOSYLATION PATTERN IN PLANT CELLS
A method of modifying a glycosylation pattern of a polypeptide-of-interest in a plant or plant cell is provided. The method comprising expressing in a plant or plant cell transformed to express at least one glycosidase in a subcellular compartment, a nucleic acid sequence encoding the polypeptide-of-interest, such that the at least one glycosidase and the polypeptide-of-interest are co-localized to the subcellular compartment of the plant or plant cell, thereby modifying the glycosylation pattern of the polypeptide-of-interest in the plant or plant cell.
USE OF ENZYME THAT CLEAVES BOTH ALPHA- AND BETA-1,4-GLYCOSIDIC BONDS
The present invention relates to use of an enzyme that cleaves both alpha- and beta-1,4-glycosidic bonds and, more particularly, the present invention provides α-L-fucosidase which has α-1,4-glucosidase and β-1,4-galactosidase activities and thus is capable of producing glucose and/or galactose, which are monosaccharides, from non-fucosylated saccharides. The enzyme has transglycosylation activity and thus produces maltooligosaccharides having a higher degree of polymerization than maltooligosaccharides used as a substrate, thereby being applicable to the development of high-value-added new materials in the food industry.
Methods for modifying human antibodies by glycan engineering
Modified Fc regions of antibodies and antibody fragments, both human and humanized, and having enhanced stability and efficacy, are provided. Fc regions with core fucose residues removed, and attached to oligosaccharides comprising terminal sialyl residues, are provided. Antibodies comprising homogeneous glycosylation of Fc regions with specific oligosaccharides are provided. Fc regions conjugated with homogeneous glycoforms of monosaccharides and trisaccharides, are provided. Methods of preparing human antibodies with modified Fc using glycan engineering, are provided.
ANTI-CD20 GLYCOANTIBODIES AND USES THEREOF
The present disclosure relates to a novel class of anti-CD20 monoclonal antibodies comprising a homogeneous population of anti-CD20 IgG molecules having the same N-glycan on each of Fc. The antibodies of the invention can be produced from anti-CD20 monoclonal antibodies by Fc glycoengineering. Importantly, the antibodies of the invention have improved therapeutic values with increased ADCC activity and increased Fc receptor binding affinity compared to the corresponding monoclonal antibodies that have not been glycoengineered.