侧翼残基对嵌合肽表位呈递的差异影响。
Differential effects of flanking residues on presentation of epitopes from chimeric peptides.
作者信息
Bergmann C C, Tong L, Cua R, Sensintaffar J, Stohlman S
机构信息
Department of Neurology, University of Southern California School of Medicine, Los Angeles 90033.
出版信息
J Virol. 1994 Aug;68(8):5306-10. doi: 10.1128/JVI.68.8.5306-5310.1994.
Abstract
Chimeric peptides in which the optimal H-2d mouse hepatitis virus nucleocapsid (pN) and human immunodeficiency virus type 1 (p18) epitopes, separated by 38, 7, or 2 amino acids, were expressed from a single open reading frame by using recombinant vaccinia viruses to analyze antigen processing of proximal class I-restricted epitopes. Recognition of the carboxy-terminal Dd-restricted p18 epitope was independent of the amino-terminal flanking residues. By contrast, proximity of the carboxy-terminal epitope decreased recognition of the amino-terminal Ld-restricted pN epitope. Immunization resulted in the induction of both p18- and pN-specific antiviral cytotoxic T lymphocytes, irrespective of the number of amino acids separating the epitopes.
摘要
通过重组痘苗病毒从单个开放阅读框表达嵌合肽，其中最佳的H-2d小鼠肝炎病毒核衣壳（pN）和1型人类免疫缺陷病毒（p18）表位被38、7或2个氨基酸隔开，以分析近端I类限制性表位的抗原加工。羧基末端Dd限制性p18表位的识别与氨基末端侧翼残基无关。相比之下，羧基末端表位的接近度降低了氨基末端Ld限制性pN表位的识别。免疫诱导了p18和pN特异性抗病毒细胞毒性T淋巴细胞，而不管分隔表位的氨基酸数量如何。
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