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Related Concept Videos

Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Antibody Structure and Classes01:25

Antibody Structure and Classes

Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
Transcytosis of IgG01:15

Transcytosis of IgG

Transcytosis is the process in which molecules are internalized by endocytosis, transported across the cell, and released through exocytosis from the opposite end of the cell. Molecules such as insulin, immunoglobulins, and certain nutrients are transferred through the recycling endosomes by recycling and transcytosis.
IgG molecules from a mother undergo transcytosis starting around 13 weeks of gestation. The amount of IgG transferred and entering the fetal blood circulation increases with...
The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques

Published on: July 5, 2018

Post-translational modifications differentially affect IgG1 conformation and receptor binding.

Damian Houde1, Yucai Peng, Steven A Berkowitz

  • 1Biogen Idec, Inc., Cambridge, Massachusetts 02142, USA.

Molecular & Cellular Proteomics : MCP
|January 28, 2010
PubMed
Summary

Post-translational modifications (PTMs) alter antibody structure and function. Methionine oxidation and galactosylation impact IgG1 conformation and FcgammaRIIIa receptor binding, while fucosylation has minimal effect.

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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Antibody Binding Specificity for Kappa (Vκ) Light Chain-containing Human (IgM) Antibodies: Polysialic Acid (PSA) Attached to NCAM as a Case Study
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Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
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Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

Published on: February 3, 2013

Area of Science:

  • Biochemistry
  • Immunology
  • Structural Biology

Background:

  • Post-translational modifications (PTMs) significantly affect protein structure, dynamics, and function.
  • Monoclonal immunoglobulin gamma1 (IgG1) antibodies are susceptible to various PTMs, influencing their biological activity and potential for adverse responses.
  • Understanding PTM-induced conformational changes is crucial for linking functional alterations to specific protein regions.

Purpose of the Study:

  • To investigate the impact of differential galactosylation, methionine oxidation, and fucosylation on IgG1 solution conformation.
  • To probe the effects of these PTMs on IgG1 binding to the FcgammaRIIIa receptor.
  • To correlate PTM-induced conformational changes with functional consequences, specifically receptor binding.

Main Methods:

  • Hydrogen/deuterium exchange mass spectrometry (HDX-MS) was employed to analyze solution conformation changes.
  • FcgammaRIIIa receptor binding assays were conducted to assess functional consequences.
  • Comparative analysis of modified and unmodified IgG1 antibodies was performed.

Main Results:

  • Methionine oxidation and galactosylation were found to significantly alter IgG1 conformation.
  • Fucosylation demonstrated little to no impact on IgG1 conformation.
  • FcgammaRIIIa receptor binding was markedly influenced by glycan composition (galactose, fucose) and PTM-induced conformational shifts.

Conclusions:

  • Specific PTMs like methionine oxidation and galactosylation induce conformational changes in IgG1 antibodies.
  • These conformational alterations, along with glycan structure, play a critical role in FcgammaRIIIa receptor engagement.
  • HDX-MS is a valuable tool for dissecting PTM-specific conformational and functional effects in complex proteins like IgG1.