Journal of Undergraduate Research
Keywords
LLO56, high affinity t-cell receptor, pathogen specific
College
Life Sciences
Department
Microbiology and Molecular Biology
Abstract
CD4+ helper T-cells play a vital role in the body’s immune response. When infectious agents attack the body, phagocytes engulf these invaders and present a peptide segment of the pathogen on a receptor (called MHCII). These receptors are located on the surface of the cell and the displayed peptide is termed an epitope. CD4+ T-cells with T-cell receptors (TCRs) specific for the displayed peptide bind to the MHCII complex. It is this binding that releases chemical signals to initiate an immune response. A disadvantage of TCRs is that their wild-type affinity for MHC is low and that they are membrane bound; not normally being secreted from the T-cell membrane. TCRs that are soluble, stable independent of the cell membrane, and have high affinity for a certain epitope can be localized at the area of infection for a longer period of time. The overall purpose of this project is to engineer a stable, soluble, high affinity T-cell receptor for the epitope from a specific bacterium (Listeria monocytogenes). The hypothesis is that developing these high affinity, soluble receptors will improve TCR targeting to a specific epitope and enable enhancement of the immune system. This could allow for the development of future therapeutics targeting the epitopes of cancers, autoimmune diseases, and viral infections.
Recommended Citation
Hancock, John and Weber, Dr. Scott
(2015)
"Engineering a Pathogen Specific High Affinity T-Cell Receptor Called LLO56,"
Journal of Undergraduate Research: Vol. 2015:
Iss.
1, Article 137.
Available at:
https://scholarsarchive.byu.edu/jur/vol2015/iss1/137