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Orientation-dependent CD45 inhibition with viral and engineered ligands. | LitMetric

AI Article Synopsis

  • CD45 is a crucial protein on T cells that regulates their signaling but doesn't have a known natural binding partner.
  • An adenovirus protein, E3/49K, binds to CD45, disrupting its signaling and helping the virus evade the immune response by forcing CD45 into dimers.
  • Researchers have created surrogate ligands based on the E3/49K mechanism to manipulate CD45's activity, illustrating that even without a known ligand, CD45's function can be altered to influence T cell responses.

Article Abstract

CD45 is a cell surface phosphatase that shapes the T cell receptor signaling threshold but does not have a known ligand. A family of adenovirus proteins, including E3/49K, exploits CD45 to evade immunity by binding to the extracellular domain of CD45, resulting in the suppression of T cell signaling. We determined the cryo-EM structure of this complex and found that the E3/49K protein is composed of three immunoglobulin domains assembled as "beads on a string" that compel CD45 into a closely abutted dimer by cross-linking the CD45 D3 domain, leading to steric inhibition of its intracellular phosphatase activity. Inspired by the E3/49K mechanism, we engineered CD45 surrogate ligands that can fine-tune T cell activation by dimerizing CD45 into different orientations and proximities. The adenovirus E3/49K protein has taught us that, despite a lack of a known ligand, CD45 activity can be modulated by extracellular dimerizing ligands that perturb its phosphatase activity and alter T cell responses.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11537708PMC
http://dx.doi.org/10.1126/sciimmunol.adp0707DOI Listing

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