Measuring interactions of MHC class I molecules using surface plasmon resonance

• Published in: Journal of immunological methods Vol. 183; no. 1; pp. 77 - 94
• Main Authors: Khilko, Sergei N., Jelonek, Marie T., Corr, Maripat, Boyd, Lisa F., Bothwell, Alfred L.M., Margulies, David H.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 14.06.1995
• Subjects: AIDS/HIV; Animals; Antibodies, Monoclonal - immunology; Antigen-Presenting Cells - immunology; Biosensing Techniques; CD8-Positive T-Lymphocytes - immunology; Epitope Mapping; Histocompatibility Antigens Class I - immunology; Humans; Kinetics; Major histocompatibility complex; Mice; Monoclonal antibody; Receptors, Antigen, T-Cell - immunology; Spectrum Analysis - instrumentation; Spectrum Analysis - methods; Surface plasmon resonance; k dis, kinetic dissociation rate constant; k ass, kinetic association rate constant; k obs, concentration dependent observed kinetic association rate constant; MHC-I, major histocompatibility complex encoded class I molecule; mAb, monoclonal antibody; HBS, Hepes buffered saline; Monoclonal antibody; SMCC, sulfosuccinimidyl-4-( N-maleimidomethyl)cyclohexane-1-carboxylate; MHC, major histocompatibility complex; Major histocompatibility complex; RU, resonance units; APC, antigen presenting cell; K d, equilibrium dissociation constant; Surface plasmon resonance; β 2m, β 2-microglobulin; SPR, surface plasmon resonance; TCR, T cell receptor

To examine the molecular interactions between major histocompatibility complex (MHC)-encoded molecules and peptides, monoclonal antibodies (mAbs), or T cell receptors, we have developed model systems employing genetically engineered soluble MHC class I molecules (MHC-I), synthetic peptides, purified...