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This article is original from Translational Medicine Network, please indicate the source for reprinting
Author: Jeff
Introduction: Interactions between T-cell receptors (TCRs) and peptide major histocompatibility complex (pMHC) ligands are usually mediated by non-covalent bonds
Researchers have identified a new mechanism by which T cells can respond to lower doses of antigen
#Sec9
'Accelerating' T cells
01
While immunotherapy is a big step forward in treating some cancers and autoimmune diseases, this type of treatment doesn't work for many patients
The team observed a previously unobserved immune interaction that had been invisible because T cell activation levels were above the threshold that normally causes these T cells to be 'deleted' from the immune system
TCR-pMHC interaction
02
The interactions between TCR and pMHC ligands are very diverse, but the physiological TCR-pMHC interactions involving covalent bonds are unknown
Since the kinetic schooling model assumes that T-cell activation requires the TCR-pMHC complex to persist long enough to activate TCR signaling, this model is sufficient to explain why long-lived, covalently bound TCR-pMHC complexes trigger T-cell activation
T cell activation
03
Here, by introducing Cys substitutions into a previously described mouse TCR, we show that Cys residues at the top of CDR3α or CDR3β are sufficient to redirect T cell fate in vivo
Furthermore, by introducing amino acid substitutions in peptide epitopes, the researchers demonstrated SS bond formation between the TCR and various pMHC ligands
References:
https://medicalxpress.
Note: This article is intended to introduce the progress of medical research and cannot be used as a reference for treatment plans
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