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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

7.7K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Antibody Structure01:10

Antibody Structure

61.8K
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...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Proteoglycans01:05

Proteoglycans

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.1K
Antibody Actions01:26

Antibody Actions

1.6K
Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
1.6K
Antibody Structure and Classes01:25

Antibody Structure and Classes

6.1K
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.
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Related Experiment Video

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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
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Sweet Rules: Linking Glycosylation to Antibody Function.

Falk Nimmerjahn1,2, Anja Werner3

  • 1Chair of Genetics, Department of Biology, Institute of Genetics, University of Erlangen-Nürnberg, Erlangen, Germany. falk.nimmerjahn@fau.de.

Experientia Supplementum (2012)
|October 23, 2021
PubMed
Summary

Antibody glycosylation significantly impacts immune responses and therapeutic potential. Understanding how sugar residues on immunoglobulin G (IgG) are regulated and function is key to developing innovative treatments for cancer and autoimmune diseases.

Keywords:
Antibody glycosylationB cellsFc-receptorsTherapeutic antibodies

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Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells
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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
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Area of Science:

  • Immunology
  • Glycobiology
  • Therapeutic Antibodies

Background:

  • Antibodies are crucial for immunity and are widely used in therapies for cancer and autoimmune diseases.
  • The fragment crystallizable (Fc) region of immunoglobulin G (IgG) contains glycosylation that modulates effector functions.
  • Understanding IgG glycosylation is vital for optimizing therapeutic antibody efficacy.

Purpose of the Study:

  • To review recent insights into the in vivo regulation of antibody glycosylation.
  • To summarize how specific sugar residues influence IgG function.
  • To highlight the clinical implications of antibody glycosylation research.

Main Methods:

  • Literature review of recent studies on IgG glycosylation.
  • Analysis of factors regulating glycosylation in vivo.
  • Examination of the impact of specific glycan structures on antibody effector functions.

Main Results:

  • Glycosylation of the IgG Fc region critically influences both pro- and anti-inflammatory activities.
  • Glycoengineered afucosylated antibodies are used in cancer therapy.
  • Sialylated antibodies are being tested for anti-inflammatory applications.

Conclusions:

  • Modulating IgG glycosylation offers a powerful strategy for therapeutic innovation.
  • Further research into IgG glycosylation regulation and function will drive the development of novel antibody-based treatments.
  • Targeting antibody glycosylation can lead to improved therapies for various diseases.