Magneto-nanosensor platform for probing low-affinity protein–protein interactions and identification of a low-affinity PD-L1/PD-L2 interaction

Jung-Rok Lee, Daniel J. B. Bechstein, Chin Chun Ooi, Ashka Patel, Richard S. Gaster, Elaine Ng, Lino C. Gonzalez and Shan X. Wang ()
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Jung-Rok Lee: Stanford University
Daniel J. B. Bechstein: Stanford University
Chin Chun Ooi: Stanford University
Ashka Patel: Genentech
Richard S. Gaster: Stanford University
Elaine Ng: Stanford University
Lino C. Gonzalez: Genentech
Shan X. Wang: Stanford University

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Substantial efforts have been made to understand the interactions between immune checkpoint receptors and their ligands targeted in immunotherapies against cancer. To carefully characterize the complete network of interactions involved and the binding affinities between their extracellular domains, an improved kinetic assay is needed to overcome limitations with surface plasmon resonance (SPR). Here, we present a magneto-nanosensor platform integrated with a microfluidic chip that allows measurement of dissociation constants in the micromolar-range. High-density conjugation of magnetic nanoparticles with prey proteins allows multivalent receptor interactions with sensor-immobilized bait proteins, more closely mimicking natural-receptor clustering on cells. The platform has advantages over traditional SPR in terms of insensitivity of signal responses to pH and salinity, less consumption of proteins and better sensitivities. Using this platform, we characterized the binding affinities of the PD-1—PD-L1/PD-L2 co-inhibitory receptor system, and discovered an unexpected interaction between the two known PD-1 ligands, PD-L1 and PD-L2.

Date: 2016
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DOI: 10.1038/ncomms12220

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