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首页> 美国卫生研究院文献>Proceedings of the National Academy of Sciences of the United States of America >Differential proteasomal processing of hydrophobic and hydrophilic protein regions: Contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef
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Differential proteasomal processing of hydrophobic and hydrophilic protein regions: Contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef

机译：疏水和亲水蛋白区域的差异蛋白酶体加工：对HIV-1-Nef中细胞毒性T淋巴细胞表位簇的贡献

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摘要

HIV proteins contain a multitude of naturally processed cytotoxic T lymphocyte (CTL) epitopes that concentrate in clusters. The molecular basis of epitope clustering is of interest for understanding HIV immunogenicity and for vaccine design. We show that the CTL epitope clusters of HIV proteins predominantly coincide with hydrophobic regions, whereas the noncluster regions are predominantly hydrophilic. Analysis of the proteasomal degradation products of full-length HIV-Nef revealed a differential sensitivity of cluster and noncluster regions to proteasomal processing. Compared with the epitope-scarce noncluster regions, cluster regions are digested by proteasomes more intensively and with greater preference for hydrophobic P1 residues, resulting in substantially greater numbers of fragments with the sizes and COOH termini typical of epitopes and their precursors. Indeed, many of these fragments correspond to endogenously processed Nef epitopes and/or their potential precursors. The results suggest that differential proteasomal processing contributes importantly to the clustering of CTL epitopes in hydrophobic regions.
机译：HIV蛋白包含大量自然加工的细胞毒性T淋巴细胞（CTL）表位，这些表位集中在簇中。表位簇化的分子基础对于理解HIV的免疫原性和疫苗设计非常重要。我们表明，HIV蛋白的CTL表位簇主要与疏水区域相吻合，而非簇区域主要是亲水的。对全长HIV-Nef的蛋白酶体降解产物的分析表明，簇和非簇区域对蛋白酶体加工的敏感性不同。与表位稀少的非簇区域相比，簇区域被蛋白酶体更强烈地消化，并且更优先选择疏水性P1残基，从而导致大量的片段具有表位及其前体的典型大小和COOH末端。实际上，许多这些片段对应于内源加工的Nef表位和/或其潜在的前体。结果表明，不同的蛋白酶体加工对疏水区域中CTL表位的聚集起重要作用。

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