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Related Concept Videos

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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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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
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Structural characterization of two γδ TCR/CD3 complexes.

Mohammed Hoque1, John Benji Grigg2, Trudy Ramlall2

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|January 3, 2025
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Structural analysis reveals gamma delta (γδ) T-cell receptor (TCR)/CD3 complexes are similar to alpha beta (αβ) TCRs but possess distinct mobile domains, aiding in γδ TCR-based therapy design.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • The T-cell receptor (TCR)/CD3 complex is crucial for immune responses and cancer immunotherapies.
  • Two main classes of TCR/CD3 complexes exist: alpha beta (αβ) and gamma delta (γδ).
  • While αβ TCR/CD3 structures are known, γδ TCR/CD3 structures remain less understood.

Purpose of the Study:

  • To elucidate the structural organization of γδ TCR/CD3 complexes.
  • To compare the structural dynamics of γδ TCR/CD3 complexes with αβ TCR/CD3 complexes.
  • To provide insights for developing γδ TCR-based immunotherapies.

Main Methods:

  • Cryoelectron microscopy (cryoEM) structural analysis of two γδ TCRs (G115 and 9C2) complexed with CD3 subunits.
  • Cell-based assays using γδ T-cell specific antibodies.
  • Analysis of the Vγ5Vδ1 complex formation.

Main Results:

  • The overall subunit organization of γδ TCR/CD3 complexes resembles that of αβ TCR/CD3 complexes.
  • γδ TCRs exhibit highly mobile extracellular domains (ECDs), contrasting with the rigid ECDs of αβ TCRs.
  • The Vγ5Vδ1 complex forms a dimer mediated by the TCR γ5 chain, assembling two TCR/CD3 complexes.

Conclusions:

  • γδ TCR/CD3 complexes share organizational similarities with αβ TCR/CD3 complexes but possess unique dynamic properties.
  • The mobility of γδ TCR ECDs influences antibody binding accessibility.
  • Understanding these structural features can inform the design of novel γδ TCR-based cancer therapies.