Solving the structural basis for alloantibody recognition of Asian HLA in solid organ transplantation

Transplantation1007S451-S45

Tumoral STING is required for effective anticancer immunity

10.1158/2326-6074.CRICIMTEATIAACR18-B1897

Targeting Hepatitis B Virus-Infected Cells with a T-Cell Receptor-Like Antibody▿ †

Virus-specific CD8 T cells are activated when their T-cell receptors (TCRs) recognize the specific viral peptide/major histocompatibility complex (MHC) class I (pMHC) complexes present on the surface of infected cells. Antibodies able to recognize the specific pMHC can mimic TCR specificity and both represent a valuable biological tool to visualize pMHC complexes on infected cells and serve as a delivery system for highly targeted therapies. To evaluate these possibilities, we created a monoclonal antibody able to specifically recognize a hepatitis B virus (HBV) envelope epitope (Env at positions 183 to 91 [Env183-91]) presented by the HLA-A201 molecule, and we tested its ability to recognize HBV-infected hepatocytes and to deliver a cargo to a specific target. We demonstrate that this antibody detects and visualizes the processed product of HBV proteins produced in naturally HBV-infected cells, is not inhibited by soluble HBV proteins present in patient sera, and mediates the intracellular delivery of a fluorescent molecule to target cells. Additionally, compared to CD8 T cells specific for the same HBV epitope, the TCR-like antibody has both a superior sensitivity and a specificity focused on distinct amino acids within the epitope. These data demonstrate that a T-cell receptor-like antibody can be used to determine the quantitative relationship between HBV replication and specific antigen presentation to CD8 T cells and serves as a novel therapeutic delivery platform for personalized health care for HBV-infected patients

Virus-specific T lymphocytes home to the skin during natural dengue infection

10.1126/scitranslmed.aaa0526Science Translational Medicine727

Targeting Epstein-Barr virus transformed B lymphoblastoid cells using antibodies with T-cell receptor like specificities

10.1182/blood-2016-03-707836BLOOD128101396-1407United State

Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A(star)11:01

10.1038/s41467-019-08790-1NATURE COMMUNICATIONS10

Defining the structural basis for human alloantibody binding to human leukocyte antigen allele HLA-A*11:01

Anti-human leukocyte antigen (HLA) antibodies are important mediators of alloresponses, but structural insights on antibody:HLA interaction are still lacking. Here the authors provide a 2.4 Å structure of antibody:HLA complex, and also analyse HLA features important for other HLA-interacting molecules, to enhance our understanding of alloimmunity