CHARACTERIZATION OF A NATURALLY PROCESSED MHC CLASS-II-RESTRICTED T-CELL DETERMINANT OF HEN EGG LYSOZYME
CHARACTERIZATION OF A NATURALLY PROCESSED MHC CLASS-II-RESTRICTED T-CELL DETERMINANT OF HEN EGG LYSOZYME
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DOI：
10.1038/342682a0
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发表时间：
1989-12-07
期刊：
影响因子：
64.8
通讯作者：
SETTE, A
中科院分区：
文献类型：
--
作者：
DEMOTZ, S;GREY, HM;SETTE, A
COMPELLING evidence indicates that T cells recognize complexes formed by major histocompatibility complex-encoded molecules and antigenic peptide fragments1–3. This is based largely on the ability of small synthetic peptides to substitute for naturally processed antigen in stimulating T cells. Naturally processed fragments of exogenous antigen are thought to arise by limited pro-teolytic degradation of native antigen inside acidic compartments of antigen-presenting cells3–6, but until now no physiologically processed antigen has been directly analysed. Here we report the characterization of physiologically processed antigen eluted from mouse class II major histocompatibility complex I–Edmolecules. The antigenic material corresponds to a previously described antigenic determinant of hen egg lysozyme (HEL 107–116) and has a relative molecular massMrof about 2,000. HPLC analysis identified at least two or three separate molecular species, suggesting limited, albeit significant, heterogeneity of naturally processed peptides. Finally, under our experimental conditions, it was calculated that a substantial proportion (10–40%) of I–Edmolecules were occupied by these HEL-derived antigenic determinants.
