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Related Concept Videos

Antibody Structure01:10

Antibody Structure

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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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
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Antibody Structure and Classes01:25

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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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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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Related Experiment Video

Updated: Apr 8, 2026

Optimized Negative Staining: a High-throughput Protocol for Examining Small and Asymmetric Protein Structure by Electron Microscopy
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Antibody Structure.

Robyn L Stanfield1, Ian A Wilson1

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037.

Microbiology Spectrum
|June 25, 2015
PubMed
Summary
This summary is machine-generated.

Researchers analyzed human antiviral antibody fragments (Fabs) using crystal structures. Novel structural features were identified, enabling potent and broad neutralization of viral targets.

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Area of Science:

  • Immunology
  • Structural Biology
  • Virology

Background:

  • Antibodies are crucial for adaptive immunity.
  • Antiviral antibodies are key to combating viral infections.
  • Understanding antibody structure-function relationships is vital for therapeutic development.

Purpose of the Study:

  • To outline antibody structure.
  • To highlight novel structural features of human antiviral antibody fragments (Fabs).
  • To correlate these features with potent and broad viral neutralization.

Main Methods:

  • X-ray crystallography
  • Structural analysis of human antiviral Fabs
  • Functional assays for neutralization potency and breadth

Main Results:

  • Detailed structural insights into several human antiviral Fabs.
  • Identification of unique structural characteristics within these Fabs.
  • Demonstration of potent and broad neutralization capabilities linked to these novel structures.

Conclusions:

  • Novel structural features in human antiviral Fabs contribute to their enhanced neutralization efficacy.
  • Structural biology provides critical insights into developing broadly neutralizing antiviral antibodies.
  • These findings advance the understanding of antibody-mediated antiviral immunity.