A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation
A single residue exchange within a viral CTL epitope alters proteasome-mediated degradation resulting in lack of antigen presentation
复制标题
DOI：
10.1016/s1074-7613(00)80488-4
复制
发表时间：
1996-08-01
期刊：
影响因子：
32.4
通讯作者：
Melief, C
中科院分区：
文献类型：
--
作者：
Ossendorp, F;Eggers, M;Melief, C
CTL epitope (KSPWFTTL) encoded by AKV/MCF type of murine leukemia virus (MuLV) differs from the sequence in Friend/Moloney/Rauscher (FMR) type in one residue (RSPWFTTL). CTL experiments indicated defective processing of the FMR peptide in tumor cells. Proteasome-mediated digestion of AKV/MCF-type 26-mer peptides resulted in the early generation and higher levels of epitope-containing fragments than digestion of FWR-type peptides, explained by prominent cleavage next to R in the FMR sequence. The fragments were identified as 10- and Il-mer peptides and were efficiently translocated by TAP. The naturally presented AKV/MCF peptide is the 8-mer, indicating ER peptide trimming. In conclusion, a single residue exchange can cause CTL epitope destruction by specific proteasomal cleavage.
