Azimi-Resketi Mojtaba, Akbari Mehdi, Heydaryan Saeed, Eftekhari Amirreza, Balali Javad, Shams Morteza, Sargazi Dariush
Department of Parasitology and Mycology, School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran.
Department of Parasitology, School of Medicine, Hamadan University of Medical Sciences, Hamadan, Iran.
In Silico Pharmacol. 2023 Jul 19;11(1):16. doi: 10.1007/s40203-023-00153-5. eCollection 2023.
Tropical theileriosis is a protozoan infection caused by , which significantly affects cattle worldwide. This study was aimed to analyze the TaSPAG1 protein and design a novel multi-epitope vaccine candidate. Online tools were employed for the prediction of Physico-chemical properties, antigenicity, allergenicity, solubility, transmembrane domains and signal peptide, posttranslational modification (PTM) sites, secondary and tertiary structures as well as intrinsically disordered regions, followed by identification and screening of potential linear and conformational B-cell epitopes and those peptides having affinity to bind bovine major histocompatibility complex class I (MHC-I) molecules. Next, a multi-epitope vaccine construct was designed and analyzed. This 907-residue protein was hydrophilic (GRAVY: -0.399) and acidic (pI: 5.04) in nature, with high thermotolerance (aliphatic: 71.27). Also, 5 linear and 12 conformational B-cell epitopes along with 8 CTL epitopes were predicted for TaSPAG1. The 355-residue vaccine candidate had a MW of about 35 kDa and it was antigenic, non-allergenic, soluble and stable, which was successfully interacted with cattle MHC-I molecule and finally cloned into the pET28a(+) vector. Further wet studies are required to assess the vaccine efficacy in cattle.
The online version contains supplementary material available at 10.1007/s40203-023-00153-5.
热带泰勒虫病是由[病原体名称未给出]引起的原生动物感染，在全球范围内对牛群有显著影响。本研究旨在分析TaSPAG1蛋白并设计一种新型多表位疫苗候选物。使用在线工具预测其物理化学性质、抗原性、致敏性、溶解性、跨膜结构域和信号肽、翻译后修饰（PTM）位点、二级和三级结构以及内在无序区域，随后鉴定和筛选潜在的线性和构象性B细胞表位以及那些与牛主要组织相容性复合体I类（MHC-I）分子有结合亲和力的肽段。接下来，设计并分析了一种多表位疫苗构建体。这种由907个残基组成的蛋白质本质上是亲水性的（亲水性总平均值：-0.399）且呈酸性（等电点：5.04），具有较高的耐热性（脂肪族指数：71.27）。此外，预测TaSPAG1有5个线性和12个构象性B细胞表位以及8个CTL表位。这个由355个残基组成的疫苗候选物分子量约为35 kDa，具有抗原性、无致敏性、可溶且稳定，能成功与牛MHC-I分子相互作用，最终被克隆到pET28a(+)载体中。需要进一步的实验研究来评估该疫苗对牛的有效性。
在线版本包含可在10.1007/s40203-023-00153-5获取的补充材料。
