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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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Antibody Structure and Classes01:25

Antibody Structure and Classes

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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.
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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Antibody Actions01:26

Antibody Actions

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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...
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Related Experiment Video

Updated: Jul 8, 2025

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations
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Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations

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Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains.

Sherry Wong1, Madeline E West1, Gareth J Morgan1

  • 1Boston University Amyloidosis Center, Boston University Chobanian and Avedisian School of Medicine, Boston, Massachusetts, USA.

Protein Science : a Publication of the Protein Society
|December 15, 2023
PubMed
Summary

Antibody light chain protein aggregation, linked to light chain amyloidosis, shows complex kinetics. Protein concentration and seeding influence aggregation rates, suggesting multiple species contribute to disease pathology.

Keywords:
AL amyloidosisaggregation kineticsamyloid fibrilsantibody variable domainprotein misfoldingsystemic light chain amyloidosis

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Misfolding Diseases

Background:

  • Light chain amyloidosis is a progressive disease linked to antibody light chain protein aggregation.
  • Amyloid fibrils form from light chain variable domains in non-native states, requiring unfolding from native structures.
  • Mechanistic studies often focus on intrinsically disordered peptides, leaving the role of native state unfolding less understood.

Purpose of the Study:

  • Investigate the impact of protein concentration and fibril seeding on the kinetics of light chain protein aggregation.
  • Explore the role of native state unfolding in the aggregation process of antibody light chains.
  • Characterize the complex aggregation behavior of the light chain variable domain protein WIL in vitro.

Main Methods:

  • Utilized thioflavin T fluorescence to monitor aggregation kinetics.
  • Studied the aggregation of the light chain variable domain protein WIL under varying protein concentrations.
  • Assessed the effect of pre-formed fibril seeds and N- or C-terminal peptide tags on aggregation.

Main Results:

  • Aggregation rate exhibited a non-linear dependence on protein concentration, peaking at 8 μM.
  • Pre-formed fibril seeds accelerated aggregation but did not eliminate the initial lag phase.
  • Seed saturation occurred at a ratio of 1 seed per 1600 protein molecules.
  • Peptide tags modified the concentration-dependent aggregation behavior without significantly altering protein stability.

Conclusions:

  • The in vitro aggregation of light chain proteins is complex, involving multiple species and influenced by concentration and seeding.
  • Native state unfolding plays a critical role in light chain aggregation, distinct from intrinsically disordered peptide self-assembly.
  • Understanding these complex aggregation dynamics is crucial for elucidating amyloid pathology in patients.