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January 1, 1997The Journal of Immunology

The EBV IL-10 homologue is a selective agonist with impaired binding to the IL-10 receptor

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Authors

YLY LiuPalo Alto InstituteRMRené de Waal MalefytSynthego (United States)FBFrancine BrièreLeiden University

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Implication

In vitro study demonstrates that Epstein-Barr virus interleukin-10 exhibits reduced receptor affinity yet retains selective agonist activity, suggesting the presence of an additional receptor subunit.

Key Points

  • To determine the binding affinity and functional receptor interactions of the Epstein-Barr virus interleukin-10 homologue relative to human interleukin-10.
  • Measured binding interactions of vIL-10His6 and hIL-10 with recombinant mouse and human IL-10 receptors.
  • Assayed cellular proliferation and cytokine responses across Ba/F3 transfectants, TF1-hIL-10R cells, human CD4+ T cell clones, and peripheral blood cells.
  • Employed an anti-hIL-10R monoclonal antibody (3F9) and soluble hIL-10R to evaluate receptor-mediated neutralization.
  • Viral IL-10 displayed an approximately 1000-fold lower affinity for recombinant IL-10R and a 1000-fold reduced potency for inhibiting IL-2 production in CD4+ T cell clones compared to human IL-10.
  • Viral IL-10 stimulated proliferation in BaF-mIL-10R and TF1-hIL-10R cells with a specific activity comparable to or greater than human IL-10, though BaF-hIL-10R cells were 1000-fold less sensitive to vIL-10.
  • Monoclonal antibody 3F9 blocked signaling by both ligands, whereas soluble hIL-10R selectively neutralized human IL-10, indicating viral IL-10 acts as a selective agonist requiring IL-10R alpha and potentially an additional receptor subunit.

Cite This Study

Liu et al. (1997) studied this question.

synapsesocial.com/papers/6a82ddec1a33da52dd1c2e79https://doi.org/10.4049/jimmunol.158.2.604
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