Disclosed are methods and compositions using glycoside hydrolases, such as an alpha-L-fucosidases, to prevent and/or treat a pathogenic infection and/or diarrhea in an animal wherein the pathogenic infection is caused by a pathogen capable of binding to an animal intestinal cell wherein said binding of the pathogen is dependent on the presence of a pathogen binding site having at least one glycan structure substituted with at least one alpha-1,2-L-fucose moiety comprising administering to the animal an effective amount of a glycoside hydrolase capable of removing the at least one alpha-1,2-L-fucose moiety from the pathogen binding site.

Disclosed are methods and compositions using glycoside hydrolases, such as an alpha-L-fucosidases, to prevent and/or treat a pathogenic infection and/or diarrhea in an animal wherein the pathogenic infection is caused by a pathogen capable of binding to an animal intestinal cell wherein said binding of the pathogen is dependent on the presence of a pathogen binding site having at least one glycan structure substituted with at least one alpha-1,2-L-fucose moiety comprising administering to the animal an effective amount of a glycoside hydrolase capable of removing the at least one alpha-1,2-L-fucose moiety from the pathogen binding site.

The present disclosure provides a fusion protein comprising a fucosidase or a truncated fragment or a mutant thereof fuses with either N-terminal end or C-terminal end of the endoglycosidase or a truncated fragment of mutant thereof. The present disclosure also provides a nucleic acid molecule expressing the fusion protein and a method for remodeling a glycan of an antibody Fc region.

The present disclosure provides a fusion protein comprising a fucosidase or a truncated fragment or a mutant thereof fuses with either N-terminal end or C-terminal end of the endoglycosidase or a truncated fragment of mutant thereof. The present disclosure also provides a nucleic acid molecule expressing the fusion protein and a method for remodeling a glycan of an antibody Fc region.

Genetically engineered host animal cells capable of producing glycoproteins having modified glycosylation patterns, e.g., defucosylation and/or monoglycosylation. Such host animal cells can be engineered to express fucosidase, endoglycosidase or both.

The present disclosure relates to glycoproteins, particularly monoclonal antibodies, comprising a glycoengineered Fc region, wherein said Fc region comprises an optimized N-glycan having the structure of Sia.sub.2(2-6)Gal.sub.2GlcNAc.sub.2Man.sub.3GlcNAc.sub.2. The glycoengineered Fc region binds FcRIIA or FcRIIIA with a greater affinity, relative to comparable monoclonal antibodies comprising the wild-type Fc region. The monoclonal antibodies of the invention are particularly useful in preventing, treating, or ameliorating one or more symptoms associated with a disease, disorder, or infection where an enhanced efficacy of effector cell function (e.g., ADCC) mediated by FcR is desired, e.g., cancer, autoimmune, infectious disease, and in enhancing the therapeutic efficacy of therapeutic antibodies the effect of which is mediated by ADCC.

The present disclosure relates to a novel class of anti-HER2 monoclonal antibodies comprising a homogeneous population of anti-HER2 IgG molecules having the same N-glycan on each of Fc. The antibodies of the invention can be produced from anti-HER2 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.

Disclosed are methods and compositions using glycoside hydrolases, such as an alpha-L-fucosidases, to prevent and/or treat a pathogenic infection and/or diarrhea in an animal wherein the pathogenic infection is caused by a pathogen capable of binding to an animal intestinal cell wherein said binding of the pathogen is dependent on the presence of a pathogen binding site having at least one glycan structure substituted with at least one alpha-1,2-L-fucose moiety comprising administering to the animal an effective amount of a glycoside hydrolase capable of removing the at least one alpha-1,2-L-fucose moiety from the pathogen binding site.

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.

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.