Technology
Background
The onset of cancer or intracellular pathogen infection correlates with the expression of viral or cellular oncogenes, ineffectual tumor suppressor activity and aberrant protein processing not consistent with healthy cell metabolism. These intracellular changes result in the appearance of protein antigens not normally expressed on a healthy cell or tissue type.
The immune system detects protein antigens by way of immune surveillance, a natural immunological function carried out by the Major Histocompatibility Complex class I (MHC; also known as the Human Leukocyte Antigen [HLA]). This process involves the MHC interacting with T-cell receptors (TCR) expressed on the surface of scanning T-lymphocytes. MHC class I molecules are found on nucleated human cells and presents a "snapshot" of the expressed proteins within a cell by displaying restricted peptides processed from intracellular proteins for disease diagnosis and response (see Figure 1). Recognition of non-self peptides in MHC-peptide complexes is indicative of disease status and prompts the action of CD8+ T-lymphocytes (CTLs), which control or eliminate diseased cells by releasing cytotoxic molecules and cytokines to further mobilize an immune response to the particular site of discovery.
T-Cell Receptor mimic (TCRm) Technology
Receptor Logic exclusively offers a revolutionary type of monoclonal antibody (mAb) that recognizes MHC-peptide complexes with the same specificity and sensitivity as the T-cell receptor (see Figure 2). These mAbs, referred to as T-Cell Receptor mimics (TCRms), recognize specific MHC-peptide complexes with picomolar affinity, thereby providing soluble reagents that can measure peptide (and associated antigen) expression on diseased cells and monitor immune responses. Such assays previously required costly, time consuming and complicated cell-based methods. TCRms offer important solutions to these and other challenges, including:
