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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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Type III hypersensitivity reactions occur when antigen–antibody complexes form and activate the complement system. Normally, these complexes help the clearance of antigens by phagocytes and red blood cells. However, when large numbers of immune complexes are present, they can deposit in tissues—particularly in the walls of blood vessels—leading to inflammation and tissue injury. These deposits trigger complement activation and neutrophil recruitment, resulting in serum...
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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.
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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.
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Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
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Peroxynitrite-induced structural perturbations in human IgG: A physicochemical study.

Mir Yasir Arfat1, Zarina Arif1, Sumit Kumar Chaturvedi2

  • 1Department of Biochemistry, Faculty of Medicine, Aligarh Muslim University, Aligarh, 202002, U.P., India.

Archives of Biochemistry and Biophysics
|May 24, 2016
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Peroxynitrite damages IgG, an important defense protein, altering its structure and potentially contributing to inflammatory diseases like rheumatoid arthritis. This study details these structural modifications.

Keywords:
AutoantibodyHuman IgGNitrotyrosinePeroxynitriteProtein structure

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Area of Science:

  • Biochemistry
  • Immunology
  • Protein Chemistry

Background:

  • Immunoglobulin G (IgG) is crucial for immune defense, requiring native structure for optimal function.
  • Peroxynitrite, a reactive nitrogen species, causes oxidative and nitrative damage to proteins in vivo.
  • Protein modifications by peroxynitrite are implicated in inflammatory diseases, including rheumatoid arthritis.

Purpose of the Study:

  • To investigate the structural alterations in IgG induced by peroxynitrite exposure in vitro.
  • To characterize the chemical modifications and their impact on IgG's biophysical properties.

Main Methods:

  • UV-visible spectroscopy
  • Fluorescence spectroscopy (Tryptophan, Tyrosine, ANS)
  • Circular Dichroism (CD) spectroscopy
  • Fourier-Transform Infrared (FT-IR) spectroscopy
  • Dynamic Light Scattering (DLS)
  • Differential Scanning Calorimetry (DSC)
  • SDS-PAGE

Main Results:

  • Peroxynitrite induced hyperchromicity, altered fluorescence (tryptophan quenching, ANS enhancement, tyrosine quenching, dityrosine enhancement), and changes in secondary structure (loss of β-sheet, amide band shifts).
  • FT-IR revealed new peaks, and nitrotyrosine, dityrosine, and nitrotryptophan were detected, indicating nitrative damage.
  • Modified IgG showed increased melting temperature and aggregation potential.

Conclusions:

  • Peroxynitrite significantly alters IgG structure and chemical composition.
  • These in vitro structural changes in IgG may promote the induction of autoantibodies in vivo under similar pathophysiological conditions.