Temming et al., 2019 - Google Patents
Human DC-SIGN and CD23 do not interact with human IgGTemming et al., 2019
View HTML- Document ID
- 614259018467705522
- Author
- Temming A
- Dekkers G
- van de Bovenkamp F
- Plomp H
- Bentlage A
- Szittner Z
- Derksen N
- Wuhrer M
- Rispens T
- Vidarsson G
- Publication year
- Publication venue
- Scientific reports
External Links
Snippet
The precise mechanisms underlying anti-inflammatory effects of intravenous immunoglobulin (IVIg) therapies remain elusive. The sialylated IgG fraction within IVIg has been shown to be therapeutically more active in mouse models. Functionally, it has been …
- 101700053597 FCER2 0 title abstract description 54
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
- G01N33/746—Erythropoetin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/71—Decreased effector function due to an Fc-modification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Temming et al. | Human DC-SIGN and CD23 do not interact with human IgG | |
Dekkers et al. | Decoding the human immunoglobulin G-glycan repertoire reveals a spectrum of Fc-receptor-and complement-mediated-effector activities | |
Correia | Stability of IgG isotypes in serum | |
Beyer et al. | Microheterogeneity of recombinant antibodies: analytics and functional impact | |
Dekkers et al. | Multi-level glyco-engineering techniques to generate IgG with defined Fc-glycans | |
van Osch et al. | Fc galactosylation promotes hexamerization of human IgG1, leading to enhanced classical complement activation | |
Subedi et al. | The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor | |
Boesch et al. | Highly parallel characterization of IgG Fc binding interactions | |
Dashivets et al. | Multi-angle effector function analysis of human monoclonal IgG glycovariants | |
Shields et al. | High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR | |
EP1957099B1 (en) | Reagents, methods and systems for selecting a cytotoxic antibody or variant thereof | |
Van de Bovenkamp et al. | Variable domain N-linked glycans acquired during antigen-specific immune responses can contribute to immunoglobulin G antibody stability | |
Chung et al. | An in vitro FcRn-dependent transcytosis assay as a screening tool for predictive assessment of nonspecific clearance of antibody therapeutics in humans | |
Rose et al. | Mutation of Y407 in the CH3 domain dramatically alters glycosylation and structure of human IgG | |
Kronimus et al. | IgG Fc N-glycosylation: Alterations in neurologic diseases and potential therapeutic target? | |
Dekkers et al. | Conserved FcγR-glycan discriminates between fucosylated and afucosylated IgG in humans and mice | |
Liu et al. | Impact of IgG fc‐oligosaccharides on recombinant monoclonal antibody structure, stability, safety, and efficacy | |
Gstöttner et al. | Affinity capillary electrophoresis–mass spectrometry as a tool to unravel proteoform-specific antibody–receptor interactions | |
Cambay et al. | Impact of N-glycosylation on Fcγ receptor/IgG interactions: Unravelling differences with an enhanced surface plasmon resonance biosensor assay based on coiled-coil interactions | |
Blundell et al. | Choice of host cell line is essential for the functional glycosylation of the Fc region of human IgG1 inhibitors of influenza B viruses | |
Dorion‐Thibaudeau et al. | Biotinylation of the Fcγ receptor ectodomains by mammalian cell co‐transfection: application to the development of a surface plasmon resonance‐based assay | |
Rowley et al. | Engineered hexavalent Fc proteins with enhanced Fc-gamma receptor avidity provide insights into immune-complex interactions | |
Oortwijn et al. | Monomeric and polymeric IgA show a similar association with the myeloid FcαRI/CD89 | |
Ball et al. | Antibody C region influences TGN1412-like functional activity in vitro | |
Yagi et al. | Structure and dynamics of immunoglobulin G glycoproteins |