信号肽
内质网
与抗原处理相关的转运体
抗原呈递
肽序列
MHC I级
肽
抗原处理
蛋白质分选信号
生物
生物化学
N端
细胞生物学
分子生物学
主要组织相容性复合体
基因
细胞毒性T细胞
体外
作者
Igor Bačík,Jennifer H. Cox,Robin L. Anderson,J. W. Yewdell,Jack R. Bennink
出处
期刊:Journal of Immunology
[The American Association of Immunologists]
日期:1994-01-15
卷期号:152 (2): 381-387
被引量:137
标识
DOI:10.4049/jimmunol.152.2.381
摘要
Under most circumstances, cell surface MHC class I molecules display peptides derived from a cytosolic pool of proteins. The efficient presentation of such peptides requires the functioning of two MHC gene products [TAP1 and TAP2 (transporter-associated with Ag processing 1 and 2)] that form a complex that facilitates transmembrane movement of peptides from the cytosol to the endoplasmic reticulum, the site of peptide association with class I molecules. It has been previously shown that peptides can be presented in a TAP-independent manner in association with HLA A2.1 or H-2 Kd if they are expressed COOH-terminal to an endoplasmic reticulum insertion/signal sequence derived from the adenovirus E3/19K glycoprotein (Anderson et al., 1991. J. Exp. Med. 174: 489; Eisenlohr et al., 1992. Cell 71: 963). We show that: 1) the E3/19K signal sequence greatly enhances the presentation of each of four additional peptides tested in association with H-2 Kb or Kk, 2) the E3/19K signal sequence can be substituted by a signal sequence derived from beta-IFN, and 3) the E3/19K signal sequence does not function when located at the COOH terminus of antigenic peptides. These findings indicate that first, many peptides require TAP for efficient presentation to T cells, second, expression of peptides COOH-terminal to signal sequences is a generally applicable method of bypassing the TAP-dependence of peptide presentation and third, the leader sequence does not act to bypass TAP simply by increasing the hydrophobic nature of peptides.
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