Nothing Special   »   [go: up one dir, main page]

Spearman et al., 2011 - Google Patents

The role of glycosylation in therapeutic antibodies

Spearman et al., 2011

View PDF
Document ID
7310735392436941141
Author
Spearman M
Dionne B
Butler M
Publication year
Publication venue
Antibody expression and production

External Links

Snippet

Monoclonal antibodies (Mabs) are biopharmaceuticals that are used increasingly for the treatment of a wide range of diseases such as cancer and autoimmunity. The effectiveness of therapeutic Mabs, most of which are immunoglobulin G (IgG), is dependent upon their …
Continue reading at citeseerx.ist.psu.edu (PDF) (other versions)

Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/40Immunoglobulins specific features characterized by post-translational modification
    • C07K2317/41Glycosylation, sialylation, or fucosylation
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/005Glycopeptides, glycoproteins
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/70Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
    • C07K2317/73Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
    • C07K2317/732Antibody-dependent cellular cytotoxicity [ADCC]
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/18Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/2887Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against CD20
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/70Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
    • C07K2317/72Increased effector function due to an Fc-modification
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/50Immunoglobulins specific features characterized by immunoglobulin fragments
    • C07K2317/52Constant or Fc region; Isotype
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/10Immunoglobulins specific features characterized by their source of isolation or production
    • C07K2317/14Specific host cells or culture conditions, e.g. components, pH or temperature
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K16/00Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/44Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material not provided for elsewhere, e.g. haptens, metals, DNA, RNA, amino acids
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10Transferases (2.)
    • C12N9/1048Glycosyltransferases (2.4)
    • C12N9/1051Hexosyltransferases (2.4.1)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2317/00Immunoglobulins specific features
    • C07K2317/20Immunoglobulins specific features characterized by taxonomic origin
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12PFERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P21/00Preparation of peptides or proteins
    • C12P21/02Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione

Similar Documents

Publication Publication Date Title
Costa et al. Glycosylation: impact, control and improvement during therapeutic protein production
Wang et al. Antibody glycoengineering strategies in mammalian cells
Del Val et al. Towards the implementation of quality by design to the production of therapeutic monoclonal antibodies with desired glycosylation patterns
Liu et al. The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody
Reusch et al. Fc glycans of therapeutic antibodies as critical quality attributes
Zhang et al. Challenges of glycosylation analysis and control: an integrated approach to producing optimal and consistent therapeutic drugs
Batra et al. Glycosylation of monoclonal antibody products: Current status and future prospects
Wang et al. Antibody glycosylation: impact on antibody drug characteristics and quality control
US11421209B2 (en) Cells producing Fc containing molecules having altered glycosylation patterns and methods and use thereof
van Berkel et al. N‐linked glycosylation is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG
Hristodorov et al. With or without sugar?(A) glycosylation of therapeutic antibodies
US8642292B2 (en) Process for producing molecules containing specialized glycan structures
Edwards et al. Strategies to control therapeutic antibody glycosylation during bioprocessing: Synthesis and separation
Shi et al. Recent advances in the understanding of biological implications and modulation methodologies of monoclonal antibody N‐linked high mannose glycans
Castilho et al. Processing of complex N-glycans in IgG Fc-region is affected by core fucosylation
Heffner et al. Glycoengineering of mammalian expression systems on a cellular level
JP2014517846A (en) Process for producing Fc-containing polypeptides having improved properties
Donini et al. Glycoengineering Chinese hamster ovary cells: a short history
Popp et al. Development of a pre-glycoengineered CHO-K1 host cell line for the expression of antibodies with enhanced Fc mediated effector function
Zhang et al. CHO glycosylation mutants as potential host cells to produce therapeutic proteins with enhanced efficacy
Kelly et al. Modulation of IgG1 immunoeffector function by glycoengineering of the GDP‐fucose biosynthesis pathway
Dorokhov et al. Functional role of carbohydrate residues in human immunoglobulin G and therapeutic monoclonal antibodies
García-Alija et al. Modulating antibody effector functions by Fc glycoengineering
Spearman et al. The role of glycosylation in therapeutic antibodies
Tayi et al. Solid‐Phase Enzymatic Remodeling Produces High Yields of Single Glycoform Antibodies