PROCESSED ANTIGEN BINDS TO NEWLY SYNTHESIZED MHC CLASS II MOLECULES IN ANTIGEN-SPECIFIC LYMPHOCYTES-B
PROCESSED ANTIGEN BINDS TO NEWLY SYNTHESIZED MHC CLASS II MOLECULES IN ANTIGEN-SPECIFIC LYMPHOCYTES-B
复制标题
DOI:
10.1016/0092-8674(91)90575-j
复制
发表时间:
1991-10-04
期刊:
影响因子:
64.5
通讯作者:
WATTS, C
中科院分区:
文献类型:
--
作者:
DAVIDSON, HW;REID, PA;WATTS, C
We describe the direct detection of radiolabeled antigen fragments bound to class II MHC molecules following immunoglobulin-mediated endocytosis and processing of native antigen in B lymphoblastoid cells. Tris-Tricine SDS gels revealed six distinct iodinated processing products that could be detected on class II MHC 1 hr after antigen endocytosis and persisted for at least 20 hr. These physiological processed antigen-class II complexes were remarkably stable, as judged by the fact that class II-alpha-beta dimers, which remain associated in SDS, became labeled with the same set of processed peptides. Using a lectin-binding assay, we show that these physiological processing products bind to the newly maturing population of MHC molecules rather than binding to the preexisting cell surface population; in contrast, an exogenous peptide binds predominantly to the latter population. A direct T cell-independent assay for processed peptide-MHC complex formation should facilitate additional studies on the exogenous antigen processing pathway.