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Related Concept Videos

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
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Antibody Structure01:10

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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
Antibodies consist of four polypeptide chains: two identical heavy...
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Conjugated Proteins02:50

Conjugated Proteins

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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Updated: Sep 25, 2025

Author Spotlight: A Pseudotype Virus System for Assessing Omicron Subvariants and Neutralizing Antibodies in SARS-CoV-2 Research
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Structures of Omicron spike complexes and implications for neutralizing antibody development.

Hangtian Guo1, Yan Gao2, Tinghan Li3

  • 1The State Key Laboratory of Pharmaceutical Biotechnology, School of Life Sciences, Institute of Viruses and Infectious Diseases, Chemistry and Biomedicine Innovation Center (ChemBIC), Institute of Artificial Intelligence Biomedicine, Nanjing University, Nanjing, China; Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai, China.

Cell Reports
|April 27, 2022
PubMed
Summary

The Omicron variant’s spike mutations allow SARS-CoV-2 immune evasion, but structural analysis reveals how new antibodies can be developed to target the virus effectively.

Keywords:
CP: ImmunologyCP: MicrobiologyOmicronSARS-CoV-2cryo-EM structuresimmune evasionneutralization antibodyspike

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The SARS-CoV-2 Omicron variant exhibits significant immune evasion due to numerous spike mutations.
  • This immune evasion compromises the efficacy of existing vaccines and antibody therapies.

Purpose of the Study:

  • To elucidate the structural basis of Omicron's immune evasion.
  • To understand the impact of Omicron mutations on antibody binding and viral entry.
  • To inform the development of next-generation therapeutic antibodies.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of the Omicron spike protein bound to ACE2.
  • Comparative structural analysis of Omicron, Delta, and wild-type spike proteins bound to a patient-derived antibody (510A5).
  • Biochemical binding assays and neutralization assays to assess antibody efficacy.

Main Results:

  • The cryo-EM structure reveals how Omicron spike interacts with ACE2.
  • Omicron mutations significantly attenuate binding of the 510A5 antibody, facilitating ACE2 interaction.
  • Biochemical data confirm reduced antibody binding and neutralization efficacy against Omicron.

Conclusions:

  • Omicron's mutations enable immune evasion by reducing antibody binding while maintaining ACE2 affinity.
  • Understanding these structural-antibody interactions is crucial for designing effective therapeutic antibodies against SARS-CoV-2 variants.
  • This study provides insights into potential strategies for generating broadly neutralizing antibodies.