H-2 class I histocompatibility antigen, K-B alpha chain (H-2Kb)

The H-2 class I histocompatibility antigen, K-B alpha chain (H-2Kb) is a murine major histocompatibility complex (MHC) class I molecule that plays a central role in the adaptive immune response by presenting intracellular peptides to CD8+ T cells (UniProt: P01901). A classic model for studying this process involves the presentation of the OVA257–264 peptide (SIINFEKL), an eight-amino acid epitope derived from chicken ovalbumin (PubMed: 10358156). This pathway is a frequent target of viral immunoevasion strategies; for instance, Mouse Cytomegalovirus (MCMV) utilizes proteins such as m04, m06, and m152 to interfere with H-2Kb trafficking and surface expression (PubMed: 19190633). By preventing the stable presentation of viral or model antigens, MCMV effectively hides infected cells from cytotoxic T lymphocyte recognition. This system is widely used in immunological research to evaluate vaccine efficacy and the mechanisms of T-cell activation. Consequently, H-2Kb and its associated peptide complexes are critical targets for experimental immunotherapies and studies on host-pathogen interactions.

Other names

H2-K1MHC class I H-2KbSIINFEKL/H-2Kb complexH-2K(B)

The H-2Kb molecule binds the OVA257-264 (SIINFEKL) peptide in the endoplasmic reticulum and transports it to the cell surface for recognition by the T-cell receptor (TCR) of CD8+ T cells to initiate an adaptive immune response (PubMed: 10358156).