THE STRUCTURE OF AN ANTIGENIC DETERMINANT IN A PROTEIN
THE STRUCTURE OF AN ANTIGENIC DETERMINANT IN A PROTEIN
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DOI：
10.1016/0092-8674(84)90412-4
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发表时间：
1984-01-01
期刊：
影响因子：
64.5
通讯作者：
LERNER, RA
中科院分区：
文献类型：
--
作者：
WILSON, IA;NIMAN, HL;LERNER, RA
阐明了合成肽的免疫原性和抗原决定簇以及亲本蛋白中相应的抗原决定簇。四个决定簇由一大组抗肽单克隆抗体与短的重叠肽（7-28个氨基酸）、免疫肽（36个氨基酸）和完整的亲本蛋白（流感病毒血凝素，HA）的反应性定义。大多数也与完整蛋白质强烈反应的抗肽抗体识别1个特异性的9个氨基酸序列。该免疫显性肽决定簇位于HA三聚体结构中的亚基界面。该位点的相对不可接近性意味着抗体与蛋白质的结合是更未折叠的HA构象。该抗原决定簇不同于先前针对血凝素所描述的那些，并且清楚地证明了合成肽产生抗体的能力，所述抗体与蛋白质的非免疫原性区域相互作用，或者当蛋白质是免疫原时，与蛋白质的非免疫原性区域相互作用。
The immunogenic and antigenic determinants of a synthetic peptide and the corresponding antigenic determinants in the parent protein were elucidated. Four determinants were defined by reactivity of a large panel of antipeptide monoclonal antibodies with short, overlapping peptides (7-28 amino acids), the immunizing peptide (36 amino acids) and the intact parent protein (the influenza virus hemagglutinin, HA). The majority of the antipeptide antibodies that also react strongly with the intact protein recognize 1 specific 9 amino acid sequence. This immunodominant peptide determinant is located in the subunit interface in the HA trimeric structure. The relative inaccessibility of this site implies that antibody binding to the protein is to a more unfolded HA conformation. This antigenic determinant differs from those previously described for the hemagglutinin and clearly demonstrates the ability of synthetic peptides to generate antibodies that interact with regions of the protein not immunogenic or generally accessible when the protein is the immunogen.