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Related Experiment Videos

LICOS, a primordial costimulatory ligand?

D Brodie1, A V Collins, A Iaboni

  • 1Sir William Dunn School of Pathology, The University of Oxford, Oxford, OX1 3RE, UK.

Current Biology : CB
|April 4, 2000
PubMed
Summary

Researchers discovered a new molecule, ligand of ICOS (LICOS), that interacts with ICOS and potentially other T cell regulators. This finding reveals a novel costimulatory pathway distinct from the classical B7-1/B7-2 interactions.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • Mammalian T cell activation relies on costimulatory signals from B7-1 (CD80) and B7-2 (CD86) binding to CD28 and CTLA-4.
  • The function of the CD28-like protein ICOS in relation to the B7 pathway was previously unclear.

Purpose of the Study:

  • To investigate the molecular interactions of ICOS and determine its role in T cell costimulation.
  • To identify the ligand for ICOS and elucidate its binding characteristics.

Main Methods:

  • Protein binding assays at varying temperatures.
  • Sequence comparisons of identified molecules with known homologs.
  • Analysis of ICOS and its novel ligand interactions.

Main Results:

Related Experiment Videos

  • ICOS binds to a novel B7-related molecule, termed ligand of ICOS (LICOS).
  • LICOS exhibits specific binding to ICOS at physiological temperatures but also weakly binds CD28 and CTLA-4 at non-physiological temperatures.
  • Sequence analysis suggests LICOS is evolutionarily conserved, with homologs in avian and murine species.

Conclusions:

  • A novel costimulatory pathway involving ICOS and LICOS has been identified.
  • LICOS represents a distinct costimulatory ligand, potentially separate from the canonical B7 pathway.
  • LICOS may be the functional homolog of a primordial vertebrate costimulatory ligand.