Yadao Jeries Dylan T, Alog Amizah Coleene B, Herrera-Ong Leana Rich
Department of Biochemistry and Molecular Biology, College of Medicine, University of the Philippines Manila, Manila, Philippines.
Clin Exp Vaccine Res. 2025 Jul;14(3):229-245. doi: 10.7774/cevr.2025.14.e22. Epub 2025 Apr 14.
Developing a treatment for Nipah virus (NiV) infection is necessary due to its high fatality rate, broad host range, and unavailable licensed effective treatment. Therefore, this study aimed to identify candidate epitopes of NiV proteins as immunotherapeutic agents for vaccine development.
Immunoinformatics was used to identify conserved fragments and candidate CD8+ epitopes in all 6 structural (F, G, L, M, N, and P) and 2 of 3 nonstructural proteins (V and W). Potential cross-reactivity, toxicity, and allergenicity were assessed. The population coverage of each candidate epitope globally and in high-risk regions were analyzed. Selected epitope-human leukocyte antigen (HLA) pairs were docked to analyze binding energy and spontaneity and favorability of complex formation.
Conservation analysis of proteins F, G, L, M, N, P, V, and W resulted in 16, 11, 40, 8, 14, 41, 10, and 10 conserved fragments (≥ nonamer), respectively. One hundred and fifty-three conserved CD8+ epitopes are promiscuous binders and are likely to be good major histocompatibility complex I binders (inhibitory concentration 50 <500 nM), non-toxic, non-allergenic, and non-cross-reactive with human antigens (E-value >1.0e-30). The 3 epitopes with the highest population coverage are YMIPRTMLEF (Global=69.77%, Indonesia=49.69%, Malaysia=5.38%, Philippines=88.44%), YMYLICYGF (Philippines=88.44%) from M, and ATIPFLFLSAY (India=53.86%, Thailand=66.25%) from L. Molecular docking of selected CD8+ epitopes with HLA I allele binders showed favorable and spontaneous complex formation.
Results showed promising CD8+ T cell epitopes among the structural and nonstructural proteins of NiV, that possess safety, immunogenicity, and broad population coverage.
由于尼帕病毒（NiV）感染致死率高、宿主范围广且尚无经许可的有效治疗方法，因此开发针对该病毒感染的治疗方法很有必要。所以，本研究旨在鉴定NiV蛋白的候选表位，作为疫苗开发的免疫治疗剂。
采用免疫信息学方法，在所有6种结构蛋白（F、G、L、M、N和P）以及3种非结构蛋白中的2种（V和W）中鉴定保守片段和候选CD8 +表位。评估了潜在的交叉反应性、毒性和致敏性。分析了每个候选表位在全球和高风险地区的人群覆盖率。对选定的表位 - 人类白细胞抗原（HLA）对进行对接，以分析结合能以及复合物形成的自发性和有利性。
对F、G、L、M、N、P、V和W蛋白的保守性分析分别产生了16、11、40、8、14、41、10和10个保守片段（≥九聚体）。153个保守的CD8 +表位是多聚结合物，可能是良好的主要组织相容性复合体I结合物（抑制浓度50<500 nM），无毒、无致敏性且与人类抗原无交叉反应（E值>1.0e - 30）。人群覆盖率最高的3个表位分别是来自M蛋白的YMIPRTMLEF（全球=69.77%，印度尼西亚=49.69%，马来西亚=5.38%，菲律宾=88.44%）、YMYLICYGF（菲律宾=88.44%），以及来自L蛋白的ATIPFLFLSAY（印度=53.86%，泰国=66.25%）。选定的CD8 +表位与HLA I等位基因结合物的分子对接显示形成了有利且自发的复合物。
结果表明，在NiV的结构蛋白和非结构蛋白中存在有前景的CD8 + T细胞表位，这些表位具有安全性、免疫原性和广泛的人群覆盖率。
