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Identification and characterization of antigen-specific T lymphocytes during the course of an immune response is tedious and indirect. To address this problem, the peptide-major histocompatability complex (MHC) ligand for a given population of T cells was multimerized to make soluble peptide-MHC tetramers. Tetramers of human lymphocyte antigen A2 that were complexed with two different human immunodeficiency virus (HIV)-derived peptides or with a peptide derived from influenza A matrix protein bound to peptide-specific cytotoxic T cells in vitro and to T cells from the blood of HIV-infected individuals. In general, tetramer binding correlated well with cytotoxicity assays. This approach should be useful in the analysis of T cells specific for infectious agents, tumors, and autoantigens.

Original publication

DOI

10.1126/science.274.5284.94

Type

Journal article

Journal

Science

Publication Date

04/10/1996

Volume

274

Pages

94 - 96

Keywords

Amino Acid Sequence, Antigens, Viral, Base Sequence, CD8-Positive T-Lymphocytes, Cell Line, Coloring Agents, Epitopes, Flow Cytometry, Gene Products, gag, HIV Seropositivity, HLA-A2 Antigen, Humans, Molecular Sequence Data, Peptide Fragments, Phenotype, RNA-Directed DNA Polymerase, T-Lymphocytes, Cytotoxic, Viral Matrix Proteins