Wang Jingqiang, Wen Jie, Li Jingxiang, Yin Jianning, Zhu Qingyu, Wang Hao, Yang Yongkui, Qin E'de, You Bo, Li Wei, Li Xiaolei, Huang Shengyong, Yang Ruifu, Zhang Xumin, Yang Ling, Zhang Ting, Yin Ye, Cui Xiaodai, Tang Xiangjun, Wang Luoping, He Bo, Ma Lianhua, Lei Tingting, Zeng Changqing, Fang Jianqiu, Yu Jun, Wang Jian, Yang Huanming, West Matthew B, Bhatnagar Aruni, Lu Youyong, Xu Ningzhi, Liu Siqi
Beijing Genomics Institute, Chinese Academy of Sciences, I-Zone, Shunyi, Beijing 101300, China.
Clin Chem. 2003 Dec;49(12):1989-96. doi: 10.1373/clinchem.2003.023184.
The widespread threat of severe acute respiratory syndrome (SARS) to human life has spawned challenges to develop fast and accurate analytical methods for its early diagnosis and to create a safe antiviral vaccine for preventive use. Consequently, we thoroughly investigated the immunoreactivities with patient sera of a series of synthesized peptides from SARS-coronavirus structural proteins.
We synthesized 41 peptides ranging in size from 16 to 25 amino acid residues of relatively high hydrophilicity. The immunoreactivities of the peptides with SARS patient sera were determined by ELISA.
Four epitopic sites, S599, M137, N66, and N371-404, located in the SARS-coronavirus S, M, and N proteins, respectively, were detected by screening synthesized peptides. Notably, N371 and N385, located at the COOH terminus of the N protein, inhibited binding of antibodies to SARS-coronavirus lysate and bound to antibodies in >94% of samples from SARS study patients. N385 had the highest affinity for forming peptide-antibody complexes with SARS serum.
Five peptides from SARS structural proteins, especially two from the COOH terminus of the N protein, appear to be highly immunogenic and may be useful for serologic assays. The identification of these antigenic peptides contributes to the understanding of the immunogenicity and persistence of SARS coronavirus.
严重急性呼吸综合征（SARS）对人类生命构成的广泛威胁引发了诸多挑战，即要开发出快速准确的早期诊断分析方法，并研制出用于预防的安全抗病毒疫苗。因此，我们深入研究了一系列源自SARS冠状病毒结构蛋白的合成肽与患者血清的免疫反应性。
我们合成了41种肽，其氨基酸残基数量在16至25个之间，具有较高的亲水性。通过酶联免疫吸附测定法（ELISA）测定这些肽与SARS患者血清的免疫反应性。
通过筛选合成肽，我们分别在SARS冠状病毒的S、M和N蛋白中检测到了四个表位位点，即S599、M137、N66和N371 - 404。值得注意的是，位于N蛋白COOH末端的N371和N385抑制了抗体与SARS冠状病毒裂解物的结合，并与94%以上的SARS研究患者样本中的抗体结合。N385与SARS血清形成肽 - 抗体复合物的亲和力最高。
来自SARS结构蛋白的五种肽，尤其是来自N蛋白COOH末端的两种肽，似乎具有高度免疫原性，可能对血清学检测有用。这些抗原肽的鉴定有助于理解SARS冠状病毒的免疫原性和持久性。
