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Related Concept Videos

Antibody Actions01:26

Antibody Actions

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.
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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.
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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.
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Constant domain-regulated antibody catalysis.

Gopal Sapparapu1, Stephanie Planque, Yukie Mitsuda

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Antibodies can act as catalysts. Researchers found that immunoglobulin M (IgM) antibodies exhibit superior catalytic activity in breaking amide and peptide bonds compared to immunoglobulin G (IgG) antibodies.

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Area of Science:

  • Immunology
  • Biochemistry
  • Structural Biology

Background:

  • Antibodies possess catalytic capabilities through their variable (V) domains.
  • The constant domain scaffold influences the catalytic efficiency of antibody V domains.

Purpose of the Study:

  • To compare the catalytic activity of antibody V domains when expressed in IgM versus IgG constant domain scaffolds.
  • To investigate the effect of the scaffold on amide and peptide bond hydrolysis.

Main Methods:

  • Recombinant expression of identical heavy and light chain V domains in both IgM and IgG constant domain scaffolds.
  • Assays using a model peptide and HIV gp120 to measure hydrolytic activity.
  • Inhibition studies using an electrophilic phosphonate diester to probe the catalytic mechanism.

Main Results:

  • The same V domains exhibited superior amide and peptide bond-hydrolyzing activity when scaffolded in IgM compared to IgG.
  • Catalytic activity was confirmed using substrates that do not require high-affinity epitope binding and one that does.
  • Inhibition by a phosphonate diester suggests a nucleophilic catalytic mechanism.
  • Monoclonal and polyclonal IgM showed significantly higher hydrolytic activity than their IgG counterparts.

Conclusions:

  • The IgM constant domain scaffold favorably affects the integrity and function of the V-domain catalytic site.
  • Antibody catalysis is a fundamental immune function, potentially more prominent in early-stage IgM antibodies.
  • Findings provide a structural basis for understanding antibody catalysis as an innate immune mechanism.