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Related Concept Videos

T Cell Activation and Clonal Selection01:22

T Cell Activation and Clonal Selection

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T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
Naive T cells that have not yet encountered an antigen express two primary CD...
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Immunoglobulin-like Cell Adhesion Molecules01:31

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

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The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
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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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NF-κB-dependent Signaling Pathway02:26

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The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
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Intracellular Signaling Affects Focal Adhesions01:17

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Related Experiment Video

Updated: Oct 13, 2025

Assessment of Human Natural Killer Cell Events Driven by FcγRIIIa Engagement in the Presence of Therapeutic Antibodies
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Fc Binding by FcγRIIa Is Essential for Cellular Activation by the Anti-FcγRIIa mAbs 8.26 and 8.2.

Bruce D Wines1,2,3, Halina M Trist1, Sandra Esparon1

  • 1Immune Therapies Laboratory, Burnet Institute, Melbourne, VIC, Australia.

Frontiers in Immunology
|November 11, 2021
PubMed
Summary

Monoclonal antibodies activate FcγRIIa receptors only when both Fab and Fc regions bind simultaneously to the same receptor. This finding is crucial for designing effective therapeutic monoclonal antibodies targeting FcγRIIa.

Keywords:
Fc receptorFcγRIIaIgGantibody dependent cellular cytotoxicity (ADCC)effector functionmAb - monoclonal antibody

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A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies
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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation
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Use of Single Chain MHC Technology to Investigate Co-agonism in Human CD8+ T Cell Activation

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Area of Science:

  • Immunology
  • Antibody Engineering
  • Cell Signaling

Background:

  • Fcγ receptor (FcγR) activity is central to antibody functions in immunity, autoimmunity, and therapeutic monoclonal antibody (mAb) efficacy.
  • The precise molecular requirements for FcγR activation by agonistic mAbs are not fully understood.

Purpose of the Study:

  • To investigate the specific properties of non-blocking mAbs (8.26 and 8.2) required for activating the human FcγRIIa.
  • To elucidate the roles of Fab and Fc regions of mAbs in FcγRIIa-mediated cell activation.

Main Methods:

  • Utilized mutant FcγRIIa receptors with inactivated Fc binding sites or altered epitopes recognized by mAbs.
  • Employed co-expression systems to segregate Fab and Fc binding interactions onto different receptor molecules.
  • Assessed receptor activation by analyzing the binding interactions of intact and fragmented mAbs.

Main Results:

  • Crosslinking FcγRIIa with mAb F(ab')2 fragments alone did not induce activation, indicating Fc region engagement is necessary.
  • Inactivation of the Fc binding site prevented activation, confirming the requirement for Fc-receptor interaction.
  • Simultaneous engagement of both Fab and Fc regions of mAb 8.26 with the same FcγRIIa molecule was essential for receptor activation.
  • Differences in epitope recognition were observed between mAbs 8.26 and 8.2.

Conclusions:

  • FcγRIIa activation by agonistic mAbs necessitates simultaneous binding of both the Fab and Fc regions to the same receptor molecule.
  • Understanding these molecular interactions is key to optimizing the design of therapeutic mAbs for improved efficacy.