Tcr Binding
Tcr Binding - Related Videos
19:05
Measuring TCR-pMHC Binding In Situ using a FRET-based Microscopy Assay
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Cited by 9 •
2015
This manuscript describes how to conduct (single molecule) Förster Resonance Energy Transfer (FRET)- based assays to measure the binding dynamics between T-cell antigen receptor (TCR) and antigenic peptide-loaded MHC molecules as they occur within the immunological synapse of a T-cell in contact with a functionalized planar supported lipid bilayer.
06:42
Identifying Kinase Inhibitors that Modulate the Thymocyte Response to Strong TCR Signals
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2025
In this video, we describe a method to identify the small-molecule kinase inhibitors that modulate the apoptosis of self-reactive CD4+CD8+ double-positive immature thymocytes. Apoptosis is induced in the double-positive thymocytes by activating them with anti-CD3- and anti-CD28-coated magnetic beads; this is followed by a small-molecule inhibitor treatment and flow cytometry analysis to detect if the inhibitors modulate the apoptotic marker expression.
16:10
A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
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Cited by 13 •
2012
The compartmentalization of proteins either within the plasma membrane or into intracellular locations is one regulatory mechanism that can greatly influence signaling outcomes; hence, to understand signaling it is important to study the spatial and temporal behavior of the proteins involved. We describe here a TIRF microscopy based system to study signal transduction in T cells, but is broadly applicable.
11:21
Streamlined Single Cell TCR Isolation and Generation of Retroviral Vectors for In Vitro and In Vivo Expression of Human TCRs
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Cited by 3 •
2017
The current protocol combines single cell paired human TCR alpha and beta chain sequencing with streamlined generation of retroviral vectors compatible with in vitro and in vivo TCR expression.
02:18
The Equilibrium Binding Constant and Binding Strength
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2020
The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium: where P and L are the unbound protein and ligand, respectively, and PL is the protein-ligand complex. As the amount of bound ligand is also related to the rate of ligand binding, experiments can also determine Kb by examining the rates of protein-ligand association (kon) and dissociation (koff) using the following ratio: Thus,...
FAQs
Specificity arises from the combined molecular fit between a TCR and two features of the presented target: the antigenic peptide and the MHC molecule displaying it. Recognition therefore depends on complementary contacts across both components rather than the peptide alone. This dual requirement helps distinguish particular antigen-presenting contexts during adaptive immune responses.
CD4 or CD8 co-receptors can be recruited during the interaction and support signaling through the TCR-CD3 complex. Their involvement links recognition at the peptide-MHC interface with intracellular signaling processes that influence whether a T lymphocyte becomes activated. This makes co-receptor participation an important part of interpreting how binding produces a cellular response.
The strength and duration of the interaction help shape the outcome of T-cell recognition. Differences in these binding properties can influence activation, subsequent differentiation, and the establishment or maintenance of immune tolerance. Consequently, binding measurements provide more than evidence of recognition; they can also help relate molecular interactions to distinct functional immune states.
Measurements can characterize whether T cells recognize a particular antigenic peptide presented by MHC and can assess relevant features of that interaction, including its strength and duration. These results help connect molecular recognition with downstream immune behavior, making binding analysis useful for studying how specific T-cell populations respond to defined targets.
In infection research, TCR binding measurements help characterize pathogen-specific T-cell responses by identifying interactions directed toward relevant antigenic peptides. The same information can support evaluation of vaccine candidates, particularly when researchers need to determine whether a candidate is associated with recognition by antigen-reactive T cells. Binding analysis therefore links antigen presentation with response characterization.
Binding information can help identify T cells that react to a defined antigenic peptide-MHC target and distinguish those cells from populations without the relevant recognition pattern. Characterizing these interactions also provides context for immune-based therapies, where understanding antigen recognition, signaling support, and response strength can guide investigation of therapeutic immune activity.