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Related Concept Videos

Antibody Structure01:10

Antibody Structure

60.3K
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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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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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...
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Related Experiment Video

Updated: Jul 16, 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 & Avedisian School of Medicine, Boston, MA, USA.

Biorxiv : the Preprint Server for Biology
|September 11, 2023
PubMed
Summary

Antibody light chain protein aggregation, a hallmark of light chain amyloidosis, is complex. Protein concentration and seeding influence aggregation kinetics, suggesting multiple species contribute to disease pathology.

Keywords:
Systemic light chain amyloidosisaggregation kineticsamyloid fibrilsantibody variable domainprotein misfoldingthioflavin T

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Light chain amyloidosis is a progressive disease linked to antibody light chain protein aggregation.
  • Amyloid fibrils form from non-native light chain conformations, implying unfolding is necessary for aggregation.
  • Mechanistic studies often focus on intrinsically disordered peptides, leaving the role of native state unfolding less understood.

Approach:

  • Investigated the aggregation kinetics of a model light chain variable domain protein (WIL) in vitro.
  • Examined the influence of protein concentration and pre-formed fibril seeds on aggregation rates using thioflavin T fluorescence.
  • Assessed the impact of N- and C-terminal peptide tags on aggregation behavior.

Key Points:

  • Aggregation rate showed a non-linear dependence on protein concentration, peaking at 8 μM.
  • The presence of N- or C-terminal tags altered the concentration-dependent aggregation.
  • Pre-formed seeds accelerated aggregation but did not eliminate the initial lag phase and showed saturation.

Conclusions:

  • The complex aggregation kinetics observed in vitro suggest that multiple protein species may contribute to light chain amyloidosis pathology.
  • Native state unfolding plays a critical, yet less understood, role in the initiation of amyloid formation.
  • Understanding these complex aggregation pathways is crucial for developing therapeutic strategies for light chain amyloidosis.