Identification of a peptide binding protein that plays a role in antigen presentation
The helper T-cell response to globular proteins appears, in general, to require intracellular processing of the antigen, such that a peptide fragment containing the T-cell antigenic determinant is released and transported to and held on the surface of an Ia-expressing, antigen-presenting cell. However, the molecular details underlying these phenomena are largely unknown. The means by which antigenic peptides are anchored on the antigen-presenting cell surface was investigated. A cell surface protein is identified that was isolated by it ability to bind to a 24-amino acid peptide fragment of pigeon cytochrome c, residues 81-104, containing the major antigenic determinant for B10.A mouse T cells. This peptide binding protein, purified from (/sup 35/S)methionine-labeled cells, appears as two discrete bands of approx. =72 and 74 kDa after NaDodSO/sub 4//PAGE. The protein can be eluted from the peptide affinity column with equivalent concentrations of either the antigenic pigeon cytochrome c peptide or the corresponding nonantigenic peptide of mouse cytochrome c. However, it does not bind to the native cytochromes c, either of pigeon or mouse, and thus the protein appears to recognize some structure available only in the free peptides. This protein plays a role in antigen presentation. Its expression is not major histocompatibility complex-restricted in that the blocking activity of the antisera can be absorbed on spleen cells from mice of different haplotypes. This peptide binding protein can be isolated from a variety of cell types, including B cells, T cells, and fibroblasts. The anchoring of processed peptides on the cell surface by such a protein may play a role in antigen presentation.
- Research Organization:
- Northwestern Univ., Evanston, IL (United States)
- OSTI ID:
- 5903532
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 84:6
- Country of Publication:
- United States
- Language:
- English
Similar Records
Biological characterization and partial purification of an idiotype and antigen specific T cell lymphokine
20-kDa protein associated with the murine T-cell antigen receptor is phosphorylated in response to activation by antigen or concanavalin A
Related Subjects
ANTIGENS
CONFIGURATION INTERACTION
LABELLED COMPOUNDS
PROTEINS
MOLECULAR WEIGHT
CYTOCHROMES
ELECTROPHORESIS
LYMPHOCYTES
METHIONINE
MICE
PEPTIDES
SULFUR 35
AMINO ACIDS
ANIMAL CELLS
ANIMALS
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOXYLIC ACIDS
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
DRUGS
EVEN-ODD NUCLEI
ISOTOPES
LEUKOCYTES
LIGHT NUCLEI
LIPOTROPIC FACTORS
MAMMALS
MATERIALS
NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PIGMENTS
RADIOISOTOPES
RODENTS
SOMATIC CELLS
SULFUR ISOTOPES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques