Edward Jenkins, Martin Fellermeyer, Daniel F. Heraghty, Sumana Sharma, Tanmay Mitra, Mateusz Kotowski, J Clarke, Yuan Lui, Sam Daly, Zach Marin, Debasis Banik, Markus Körbel, Emily Zhi Qing Ng, Thomas Lister, Ana Mafalda Santos, Steven F. Lee, Michael L. Dustin, Simon J. Davis, David Klenerman
Lymphocyte activation relies on the integration of signals from multiple receptors at cell-cell contacts, but the spatiotemporal regulation of this process is unclear. Here, we show that programmed cell death protein 1 (PD-1) and T cell receptor (TCR) signals are integrated at nanoscale microvillar close contacts formed during T cell interactions with their targets. PD-1 signaling begins as these contacts form and selectively limits the duration, but not the amplitude, of TCR signaling. PD-1 suppresses TCR activity directly, by locally recruiting Src homology 2 domain-containing protein tyrosine phosphatase-2 (SHP2), and indirectly, by reducing cell-spreading, close-contact formation, and TCR engagement. A PD-1 blocking antibody induced inhibitory signaling when Fc receptor engagement trapped PD-1 at close contacts. Engineering the antibody to prevent PD-1 trapping eliminated these agonistic effects and improved blockade efficacy. These findings identify microvillar contacts as crucial hubs of initial signal integration and provide a framework for optimizing checkpoint immunotherapies.