Antigen recognition by H-2-restricted T cells. II. A tryptic ovalbumin peptide that substitutes for processed antigen

Autor:	Shimonkevitz R, Colon S, Jw, Kappler, Philippa Marrack, Hm, Grey
Rok vydání:	1984
Předmět:	B-Lymphocytes Mice Inbred BALB C Lymphoma Ovalbumin Immune Sera T-Lymphocytes Immunology H-2 Antigens Histocompatibility Antigens Class II Lymphocyte Activation Peptide Fragments Mice Animals Immunology and Allergy Trypsin Amino Acid Sequence Rabbits Antigens
Zdroj:	Europe PubMed Central
ISSN:	1550-6606 0022-1767
DOI:	10.4049/jimmunol.133.4.2067
Popis:	A 17-amino acid tryptic peptide of chicken ovalbumin, designated P323-339, that substituted for processed antigen when presented by glutaraldehyde prefixed accessory cells to specific I-restricted T hybridomas was characterized. The peptide antigen could not be demonstrated to have any specific or stable interactions with accessory cell Ia antigens by either direct binding or functional assays for inhibition of specific T cell activation. In addition, the T cell receptor for I-restricted antigen had no affinity for free antigen alone. A rabbit antibody specific for the antigenic peptide inhibited presentation when introduced before but not after binding of the peptide to accessory cells. These results extend our earlier finding that accessory cell-mediated processing of chicken ovalbumin can be completely explained by the fragmentation of the native molecule into smaller m.w. peptides, and suggests that if an antigen/Ia complex is important in T cell activation, it forms significantly only in the presence of the T cell receptor for I-restricted antigen.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f78c8de1181a4659959fbf2deb1024b https://doi.org/10.4049/jimmunol.133.4.2067 Zobrazit plný text záznamu