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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...
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.

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
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Examining the non-linear relationship between monoclonal antiphospholipid antibody sequence, structure and function.

I Giles1, A Lambrianides, A Rahman

  • 1Medical Molecular Biology Unit, Institute of Child Health, University College London, London, UK. i.giles@ich.ucl.ac.uk

Lupus
|October 2, 2008
PubMed
Summary

Pathogenic antiphospholipid antibodies (aPL) in antiphospholipid syndrome (APS) bind to anionic phospholipids and beta2-glycoprotein I. Specific amino acids in antibody binding sites influence this interaction and pathogenicity, guiding diagnostic and therapeutic development.

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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

Published on: June 29, 2016

Area of Science:

  • Immunology
  • Molecular Biology
  • Rheumatology

Background:

  • Antiphospholipid syndrome (APS) involves pathogenic antiphospholipid antibodies (aPL) causing thrombosis and pregnancy morbidity.
  • These aPL bind to anionic phospholipids (PL) and beta2-glycoprotein I (beta(2)GPI).

Purpose of the Study:

  • To identify sequence motifs distinguishing pathogenic from non-pathogenic aPL.
  • To understand molecular mechanisms of target cell activation by pathogenic aPL.
  • To explore potential for improved diagnostics and therapeutics for APS.

Main Methods:

  • Sequence analysis of human monoclonal aPL.
  • In vitro antibody variant creation by altering key amino acids.
  • Molecular modeling of antigen/antibody complexes.

Main Results:

  • High-affinity binding to anionic PL and beta(2)GPI is linked to specific amino acids (arginine, asparagine, lysine) in antibody complementarity determining regions (CDRs).
  • Arginine residues significantly impact binding affinity, though effects vary by position and do not always correlate with pathogenicity.
  • Distinct sequence motifs may differentiate pathogenic aPL subsets.

Conclusions:

  • Understanding the role of specific amino acids in aPL binding and pathogenicity is crucial.
  • Molecular insights into antigen-antibody interactions can inform the development of advanced diagnostic and therapeutic strategies for APS.
  • Further research into pathogenic aPL subsets may lead to more targeted treatments.