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Fine mapping epitope on glycoprotein Gc from Crimean-Congo hemorrhagic fever virus.
Comparative Immunology, Microbiology and Infectious Diseases ( IF 2 ) Pub Date : 2019-10-19 , DOI: 10.1016/j.cimid.2019.101371
Jingyuan Zhang 1 , Adili Simayi 2 , Meifang Wang 1 , Abulimiti Moming 1 , Wangxiang Xu 3 , Chen Wang 2 , Yijie Li 1 , Juntao Ding 1 , Fei Deng 4 , Yujiang Zhang 2 , Surong Sun 1
Affiliation  

Crimean-Congo hemorrhagic fever (CCHF) is a tick-borne zoonosis, caused by CCHF virus (CCHFV) and which there are no diagnostic or therapeutic strategies. The C-terminus of glycoprotein (Gc) encoded by the CCHFV M gene is responsible for CCHFV binding to cellular receptors and acts as a neutralizing-antibody target. In this study, a modified biosynthetic peptide technique (BSP) was used to identify fine epitopes of Gc from the CCHFV YL04057 strain using rabbit antiserum against CCHFV-Gc. Six B cell epitopes (BCEs) and one antigenic peptide (AP) were identified: E1 (88VEDASES94), E2 (117GDRQVEE123), E3 (241EIVTLH246), AP-4 (281DFQVYHVGNLLRGDKV296), E5a (370GDTP QLDL377), E5b (373PQLDLKAR380), and E6 (443HVRSSD448). Western blotting analysis showed that each epitope interacted with the positive serum of sheep that had been naturally infected with CCHFV, and the results were consistent with that of Dot-ELISA. The multiple sequence alignment (MSA) revealed high conservation of the identified epitopes among ten CCHFV strains from different areas, except for epitopes AP-4 and E6. Furthermore, three-dimensional structural modeling showed that all identified epitopes were located on the surface of the Gc "head" domain. These mapped epitopes of the CCHFV Gc would provide a basis for further increase our understanding CCHFV glycoprotein function and the development of a CCHFV epitope-based diagnostics vaccine and detection antigen.

中文翻译:

克里米亚-刚果出血热病毒糖蛋白Gc上的精细定位表位。

克里米亚-刚果出血热(CCHF)是由tick传播的人畜共患病,由CCHF病毒(CCHFV)引起,尚无诊断或治疗策略。CCHFV M基因编码的糖蛋白(Gc)的C端负责CCHFV与细胞受体的结合,并充当中和抗体的靶标。在这项研究中,使用改良的生物合成肽技术(BSP)使用针对CCHFV-Gc的兔抗血清从CCHFV YL04057菌株中鉴定出Gc的精细表位。鉴定出六个B细胞表位(BCE)和一个抗原肽(AP):E1(88VEDASES94),E2(117GDRQVEE123),E3(241EIVTLH246),AP-4(281DFQVYHVGNLLRGDKV296),E5a(370GDTP QLDL377),E5b(373PQLDLKAR380和E6(443HVRSSD448)。蛋白质印迹分析表明,每个表位均与天然感染CCHFV的绵羊的阳性血清相互作用,结果与Dot-ELISA一致。多序列比对(MSA)显示,除了表位AP-4和E6外,来自不同地区的十个CCHFV菌株中已鉴定的表位高度保守。此外,三维结构建模表明,所有已识别的表位均位于Gc“头”结构域的表面。CCHFV Gc的这些定位表位将为进一步增进我们对CCHFV糖蛋白功能的了解以及开发基于CCHFV表位的诊断疫苗和检测抗原提供基础。多序列比对(MSA)显示,除了表位AP-4和E6外,来自不同地区的十个CCHFV菌株中已鉴定的表位高度保守。此外,三维结构建模表明,所有已识别的表位均位于Gc“头”结构域的表面。CCHFV Gc的这些定位表位将为进一步增进我们对CCHFV糖蛋白功能的了解以及开发基于CCHFV表位的诊断疫苗和检测抗原提供基础。多序列比对(MSA)显示,除了表位AP-4和E6外,来自不同地区的十个CCHFV菌株中已鉴定的表位高度保守。此外,三维结构建模表明,所有已识别的表位均位于Gc“头”结构域的表面。CCHFV Gc的这些定位表位将为进一步了解CCHFV糖蛋白功能以及开发基于CCHFV表位的诊断疫苗和检测抗原奠定基础。
更新日期:2019-11-01
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