ArticlePloS one2014
TCR triggering by pMHC ligands tethered on surfaces via poly(ethylene glycol) depends on polymer length.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
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- Hierarchically Multivalent Peptide-Nanoparticle Architectures: A Systematic Approach to Engineer Surface Adhesion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- The interplay between membrane topology and mechanical forces in regulating T cell receptor activity.Communications biology · 2022Review
- Nanoarchitectures for efficient IgE cross-linking on effector cells to study amoxicillin allergy.Allergy · 2021Article
- Targeting CD4Biomacromolecules · 2020Article
- Single electron transfer events and dynamical heterogeneity in the small protein azurin fromChemical science · 2019Article
- Biotin-Avidin-Mediated Capture of Microspheres on Polymer Fibers.Molecules (Basel, Switzerland) · 2019Article
- Varying PEG density to control stress relaxation in alginate-PEG hydrogels for 3D cell culture studies.Biomaterials · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Antigen recognition by T cells relies on the interaction between T cell receptor (TCR) and peptide-major histocompatibility complex (pMHC) at the interface between the T cell and the antigen presenting cell (APC). The pMHC-TCR interaction is two-dimensional (2D), in that both the ligand and receptor are membrane-anchored and their movement is limited to 2D diffusion. The 2D nature of the interaction is critical for the ability of pMHC ligands to trigger TCR. The exact properties of the 2D pMHC-TCR interaction that enable TCR triggering, however, are not fully understood. Here, we altered the 2D pMHC-TCR interaction by tethering pMHC ligands to a rigid plastic surface with flexible poly(ethylene glycol) (PEG) polymers of different lengths, thereby gradually increasing the ligands' range of motion in the third dimension. We found that pMHC ligands tethered by PEG linkers with long contour length were capable of activating T cells. Shorter PEG linkers, however, triggered TCR more efficiently. Molecular dynamics simulation suggested that shorter PEGs exhibit faster TCR binding on-rates and off-rates. Our findings indicate that TCR signaling can be triggered by surface-tethered pMHC ligands within a defined 3D range of motion, and that fast binding rates lead to higher TCR triggering efficiency. These observations are consistent with a model of TCR triggering that incorporates the dynamic interaction between T cell and antigen-presenting cell.
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