{"title":"基于免疫信息学和分子动力学模拟的高效dc诱导多表位GP350抗eb病毒疫苗的设计","authors":"Golzar Fatahi , Maasoume Abdollahi , Zahra Nashtahosseini , Shima Minoo , Mehrnaz Mostafavi , Kholoud Saeidi","doi":"10.1016/j.bbrep.2025.101966","DOIUrl":null,"url":null,"abstract":"<div><div>The findings underscore the critical role of Epstein-Barr virus (EBV) in the onset of various cancers. In response to the lack of effective treatments or vaccines for EBV infection, this investigation employed immunoinformatics approaches to develop a potent vaccine targeting multiple epitopes of the EBV glycoprotein 350 (Gp350), a key surface protein. Utilizing computational methods, we designed a comprehensive multi-epitope vaccine featuring 11 CTL and HTL epitopes, totaling 324 amino acids and covering five distinct EBV strains such as B95-8, P3HR-1, GD1, AG876, and Akata. To enhance immunogenicity, the 50S ribosomal protein L7/L12 (rplL) was included as an adjuvant at the vaccine's N-terminal. The vaccine was evaluated for its physicochemical and immunological properties, demonstrating stability, potency, solubility, hydrophilicity, non-allergenicity, and non-toxicity. Molecular docking studies have shown that the vaccine interacts with Toll-like receptor 4 (TLR4). Simulations performed using GROMACS confirmed the stability of the system over 100ns. Immune simulations indicated that the vaccine elicited robust humoral and cellular responses, activating both innate and adaptive immunity. The findings indicate that the multi-epitope vaccine is highly immunogenic and shows significant potential for further experimental validation.</div></div>","PeriodicalId":8771,"journal":{"name":"Biochemistry and Biophysics Reports","volume":"42 ","pages":"Article 101966"},"PeriodicalIF":2.3000,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Designing of an efficient DC-inducing multi-epitope vaccine against Epstein Barr virus targeting the GP350 using immunoinformatics and molecular dynamic simulation\",\"authors\":\"Golzar Fatahi , Maasoume Abdollahi , Zahra Nashtahosseini , Shima Minoo , Mehrnaz Mostafavi , Kholoud Saeidi\",\"doi\":\"10.1016/j.bbrep.2025.101966\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The findings underscore the critical role of Epstein-Barr virus (EBV) in the onset of various cancers. In response to the lack of effective treatments or vaccines for EBV infection, this investigation employed immunoinformatics approaches to develop a potent vaccine targeting multiple epitopes of the EBV glycoprotein 350 (Gp350), a key surface protein. Utilizing computational methods, we designed a comprehensive multi-epitope vaccine featuring 11 CTL and HTL epitopes, totaling 324 amino acids and covering five distinct EBV strains such as B95-8, P3HR-1, GD1, AG876, and Akata. To enhance immunogenicity, the 50S ribosomal protein L7/L12 (rplL) was included as an adjuvant at the vaccine's N-terminal. The vaccine was evaluated for its physicochemical and immunological properties, demonstrating stability, potency, solubility, hydrophilicity, non-allergenicity, and non-toxicity. Molecular docking studies have shown that the vaccine interacts with Toll-like receptor 4 (TLR4). Simulations performed using GROMACS confirmed the stability of the system over 100ns. Immune simulations indicated that the vaccine elicited robust humoral and cellular responses, activating both innate and adaptive immunity. The findings indicate that the multi-epitope vaccine is highly immunogenic and shows significant potential for further experimental validation.</div></div>\",\"PeriodicalId\":8771,\"journal\":{\"name\":\"Biochemistry and Biophysics Reports\",\"volume\":\"42 \",\"pages\":\"Article 101966\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2025-03-03\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemistry and Biophysics Reports\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2405580825000536\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemistry and Biophysics Reports","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2405580825000536","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Designing of an efficient DC-inducing multi-epitope vaccine against Epstein Barr virus targeting the GP350 using immunoinformatics and molecular dynamic simulation
The findings underscore the critical role of Epstein-Barr virus (EBV) in the onset of various cancers. In response to the lack of effective treatments or vaccines for EBV infection, this investigation employed immunoinformatics approaches to develop a potent vaccine targeting multiple epitopes of the EBV glycoprotein 350 (Gp350), a key surface protein. Utilizing computational methods, we designed a comprehensive multi-epitope vaccine featuring 11 CTL and HTL epitopes, totaling 324 amino acids and covering five distinct EBV strains such as B95-8, P3HR-1, GD1, AG876, and Akata. To enhance immunogenicity, the 50S ribosomal protein L7/L12 (rplL) was included as an adjuvant at the vaccine's N-terminal. The vaccine was evaluated for its physicochemical and immunological properties, demonstrating stability, potency, solubility, hydrophilicity, non-allergenicity, and non-toxicity. Molecular docking studies have shown that the vaccine interacts with Toll-like receptor 4 (TLR4). Simulations performed using GROMACS confirmed the stability of the system over 100ns. Immune simulations indicated that the vaccine elicited robust humoral and cellular responses, activating both innate and adaptive immunity. The findings indicate that the multi-epitope vaccine is highly immunogenic and shows significant potential for further experimental validation.
期刊介绍:
Open access, online only, peer-reviewed international journal in the Life Sciences, established in 2014 Biochemistry and Biophysics Reports (BB Reports) publishes original research in all aspects of Biochemistry, Biophysics and related areas like Molecular and Cell Biology. BB Reports welcomes solid though more preliminary, descriptive and small scale results if they have the potential to stimulate and/or contribute to future research, leading to new insights or hypothesis. Primary criteria for acceptance is that the work is original, scientifically and technically sound and provides valuable knowledge to life sciences research. We strongly believe all results deserve to be published and documented for the advancement of science. BB Reports specifically appreciates receiving reports on: Negative results, Replication studies, Reanalysis of previous datasets.