作者: Charles F. Towne , Ian A. York , Levi B. Watkin , John S. Lazo , Kenneth L. Rock
DOI: 10.4049/JIMMUNOL.178.11.6923
关键词:
摘要: Long oligopeptides (>10 residues) are generated during the catabolism of cellular proteins in cytosol. To be presented to T cells, such peptides must trimmed by aminopeptidases proper size (typically 8–10 stably bind MHC class I molecules. Aminopeptidases also destroy epitopes trimming them even shorter lengths. Bleomycin hydrolase (BH) is a cytosolic aminopeptidase that has been suggested play key role generating I-presented peptides. We show BH-deficient cells from mice unimpaired their ability present N-extended precursors or whole Ags and express normal levels Similarly, develop CD8+ cell responses eight three different viruses vivo. Therefore, BH itself not essential for generation destruction In contrast, when BH−/− crossed lacking another aminopeptidase, leucine resulting BH−/−leucine aminopeptidase−/− progeny selective increase gp276 epitope lymphocytic choriomeningitis virus, whereas respond several other unchanged. does influence presentation some Ags, although its largely redundant with aminopeptidases.