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Related Concept Videos

Antibody Structure01:10

Antibody Structure

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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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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Antibody Structure and Classes01:25

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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.
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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

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In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or...
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Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments
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Engineering disulfide bonds within an antibody.

Yoshihisa Hagihara1, Dirk Saerens2

  • 1National Institute of Advanced Industrial Science and Technology (AIST), 1-8-31 Midorigaoka Ikeda, Osaka 563-8577, Japan.

Biochimica Et Biophysica Acta
|July 20, 2014
PubMed
Summary

Antibody disulfide bonds stabilize structure but can be engineered. Removing or adding these bonds may enable intracellular antibody use and improve stability of antibody fragments without affecting antigen binding.

Keywords:
AntibodyAntibody fragmentDisulfide bondProtein engineeringProtein foldingSingle domain antibody

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Immunology

Background:

  • Antibodies possess disulfide bonds crucial for structural stability in extracellular environments.
  • Immunoglobulin G (IgG) subclasses are defined by inter-chain disulfide bond patterns.
  • Intra-domain disulfide bonds stabilize Ig-fold domains but can be replaced or engineered.

Approach:

  • Investigated amino acid substitutions (Val/Ala pairs) for cysteine replacement in Ig-fold domains.
  • Explored the introduction of additional disulfide bonds into variable domains of antibodies.
  • Assessed the impact of disulfide bond modifications on antibody structure, function, and antigen-binding affinity.

Key Points:

  • Replacing intra-domain disulfide bonds with specific amino acid pairs (e.g., Ala-Ala) can be achieved without compromising Ig-fold domain stability.
  • Engineered disulfide bonds can enhance the stability of antibody fragments like antigen-binding fragments (Fabs) and single-domain antibodies (VHHs).
  • Introducing new disulfide bonds into antibody variable regions does not necessarily reduce antigen-binding affinity.

Conclusions:

  • Disulfide bond engineering offers a strategy for stabilizing antibodies and their fragments.
  • Modifications to disulfide bonds may facilitate the intracellular application of antibodies.
  • This research contributes to the field of molecular engineering for antibody-based therapeutics.