Moballegh Naseri Mona, Shams Saeed, Moballegh Naseri Mohammad, Bakhshi Bita
Cellular and Molecular Research Center, Qom University of Medical Sciences, 3736175513, Qom, Iran.
Department of Computer and IT, Shahab-Danesh University, Qom, Iran.
BMC Res Notes. 2020 Nov 10;13(1):518. doi: 10.1186/s13104-020-05364-z.
Vaccination is an important strategy for the eradication of infectious diseases. CadF protein of Campylobacter jejuni is one of the important factors in the pathogenesis of this bacterium. The purpose of this work was to perform a bioinformatics study to identify an epitope-based CadF vaccine, as a subunit vaccine. Full protein sequences of CadF were extracted from the NCBI and UniProt databases and subjected to in silico evaluations, including sequence analysis, allergenicity, antigenicity, epitope conservancy, and molecular docking assessments done by different servers.
The results showed that CadF was a highly conserved protein belonging to the outer member proteins superfamily. Among the evaluated epitopes, LSDSLALRL was identified as an antigenic and non-allergenic peptide with a suitable structure for vaccine development. It was also able to stimulate both T and B cells. This 9-mer peptide was located in 136-144 segment of CadF protein and interacted with both HLA-A 0101 and HLA-DRB1 0101 alleles. Overall, the obtained theoretical results showed that CadF protein could be used for designing and evaluating a new effective vaccine against C. jejuni.
疫苗接种是根除传染病的重要策略。空肠弯曲菌的CadF蛋白是该细菌发病机制中的重要因素之一。本研究旨在通过生物信息学研究确定一种基于表位的CadF疫苗,作为亚单位疫苗。从NCBI和UniProt数据库中提取CadF的完整蛋白质序列,并进行计算机模拟评估,包括序列分析、致敏性、抗原性、表位保守性以及由不同服务器进行的分子对接评估。
结果表明,CadF是一种高度保守的蛋白质,属于外膜蛋白超家族。在所评估的表位中,LSDSLALRL被鉴定为一种具有适合疫苗开发结构的抗原性且无致敏性的肽。它还能够刺激T细胞和B细胞。这种9肽位于CadF蛋白的136 - 144区段,与HLA - A 0101和HLA - DRB1 0101等位基因均有相互作用。总体而言,所获得的理论结果表明,CadF蛋白可用于设计和评估一种针对空肠弯曲菌的新型有效疫苗。