Mohammed Alissa, Abdullah Alghamdi, Suad A Alghamdi, Muhammad Suleman
{"title":"基于免疫信息学的高免疫原性多表位亚单位疫苗设计以刺激针对Junin病毒的适应性免疫应答。","authors":"Mohammed Alissa, Abdullah Alghamdi, Suad A Alghamdi, Muhammad Suleman","doi":"10.1007/s11030-024-11082-6","DOIUrl":null,"url":null,"abstract":"<p><p>The Junin virus causes Argentine hemorrhagic fever, leading to severe complications such as high fever, malaise, muscle pain, and bleeding disorders, including hemorrhages in the skin and mucous membranes. Neurological issues like confusion, seizures, and coma can also occur. Without prompt and effective treatment, the disease can be fatal, with mortality rates reaching up to 30%. Taking serious measures is essential to mitigate the spread of the disease. Vaccination is the most effective choice to neutralize the Junin virus in the current situation. Consequently, to design the highly immunogenic and non-allergenic multi-epitope subunit vaccine against the Junin virus, we employed the immunoinformatic approach to screen the glycoprotein, nucleoprotein, and RDRP protein for potential immunogenic CTL (Cytotoxic T Lymphocyte), HTL (Helper T Lymphocyte) and B (B Lymphocyte) cell epitopes. Afterward, the predicted epitopes were subjected to 3D modeling and validation. The strong binding affinity of the constructed vaccines with the human TLR3 was confirmed through molecular docking, with scores of - 333 kcal/mol for glycoprotein, - 297 kcal/mol for nucleoprotein, - 308 kcal/mol for RDRP, and - 305 kcal/mol for combined vaccines. Additionally, the binding free energies recorded were - 63.54 kcal/mol, - 64.16 kcal/mol, - 56.81 kcal/mol, and - 51.52 kcal/mol, respectively. Furthermore, the dynamic stability, residual fluctuation, and compactness of vaccine-TLR-3 complexes were confirmed by the molecular dynamic simulation. The codon adaptation index (CAI) values and high GC content confirmed the stable expression of constructed vaccines in the pET-28a ( +) expression vector. The immune simulation analysis demonstrated that administering booster doses of the developed vaccines resulted in a notable increase in IgG, IgM, interleukins, and cytokines levels, indicating effective antigen clearance over time. In conclusion, our study provides preclinical evidence for designing a highly effective Junin virus vaccine, necessitating further in-vitro and in-vivo experiments.</p>","PeriodicalId":708,"journal":{"name":"Molecular Diversity","volume":" ","pages":""},"PeriodicalIF":3.9000,"publicationDate":"2024-12-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Immunoinformatic based designing of highly immunogenic multi-epitope subunit vaccines to stimulate an adaptive immune response against Junin virus.\",\"authors\":\"Mohammed Alissa, Abdullah Alghamdi, Suad A Alghamdi, Muhammad Suleman\",\"doi\":\"10.1007/s11030-024-11082-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The Junin virus causes Argentine hemorrhagic fever, leading to severe complications such as high fever, malaise, muscle pain, and bleeding disorders, including hemorrhages in the skin and mucous membranes. Neurological issues like confusion, seizures, and coma can also occur. Without prompt and effective treatment, the disease can be fatal, with mortality rates reaching up to 30%. Taking serious measures is essential to mitigate the spread of the disease. Vaccination is the most effective choice to neutralize the Junin virus in the current situation. Consequently, to design the highly immunogenic and non-allergenic multi-epitope subunit vaccine against the Junin virus, we employed the immunoinformatic approach to screen the glycoprotein, nucleoprotein, and RDRP protein for potential immunogenic CTL (Cytotoxic T Lymphocyte), HTL (Helper T Lymphocyte) and B (B Lymphocyte) cell epitopes. Afterward, the predicted epitopes were subjected to 3D modeling and validation. The strong binding affinity of the constructed vaccines with the human TLR3 was confirmed through molecular docking, with scores of - 333 kcal/mol for glycoprotein, - 297 kcal/mol for nucleoprotein, - 308 kcal/mol for RDRP, and - 305 kcal/mol for combined vaccines. Additionally, the binding free energies recorded were - 63.54 kcal/mol, - 64.16 kcal/mol, - 56.81 kcal/mol, and - 51.52 kcal/mol, respectively. Furthermore, the dynamic stability, residual fluctuation, and compactness of vaccine-TLR-3 complexes were confirmed by the molecular dynamic simulation. The codon adaptation index (CAI) values and high GC content confirmed the stable expression of constructed vaccines in the pET-28a ( +) expression vector. The immune simulation analysis demonstrated that administering booster doses of the developed vaccines resulted in a notable increase in IgG, IgM, interleukins, and cytokines levels, indicating effective antigen clearance over time. In conclusion, our study provides preclinical evidence for designing a highly effective Junin virus vaccine, necessitating further in-vitro and in-vivo experiments.</p>\",\"PeriodicalId\":708,\"journal\":{\"name\":\"Molecular Diversity\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":3.9000,\"publicationDate\":\"2024-12-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Molecular Diversity\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://doi.org/10.1007/s11030-024-11082-6\",\"RegionNum\":2,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Molecular Diversity","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1007/s11030-024-11082-6","RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Immunoinformatic based designing of highly immunogenic multi-epitope subunit vaccines to stimulate an adaptive immune response against Junin virus.
The Junin virus causes Argentine hemorrhagic fever, leading to severe complications such as high fever, malaise, muscle pain, and bleeding disorders, including hemorrhages in the skin and mucous membranes. Neurological issues like confusion, seizures, and coma can also occur. Without prompt and effective treatment, the disease can be fatal, with mortality rates reaching up to 30%. Taking serious measures is essential to mitigate the spread of the disease. Vaccination is the most effective choice to neutralize the Junin virus in the current situation. Consequently, to design the highly immunogenic and non-allergenic multi-epitope subunit vaccine against the Junin virus, we employed the immunoinformatic approach to screen the glycoprotein, nucleoprotein, and RDRP protein for potential immunogenic CTL (Cytotoxic T Lymphocyte), HTL (Helper T Lymphocyte) and B (B Lymphocyte) cell epitopes. Afterward, the predicted epitopes were subjected to 3D modeling and validation. The strong binding affinity of the constructed vaccines with the human TLR3 was confirmed through molecular docking, with scores of - 333 kcal/mol for glycoprotein, - 297 kcal/mol for nucleoprotein, - 308 kcal/mol for RDRP, and - 305 kcal/mol for combined vaccines. Additionally, the binding free energies recorded were - 63.54 kcal/mol, - 64.16 kcal/mol, - 56.81 kcal/mol, and - 51.52 kcal/mol, respectively. Furthermore, the dynamic stability, residual fluctuation, and compactness of vaccine-TLR-3 complexes were confirmed by the molecular dynamic simulation. The codon adaptation index (CAI) values and high GC content confirmed the stable expression of constructed vaccines in the pET-28a ( +) expression vector. The immune simulation analysis demonstrated that administering booster doses of the developed vaccines resulted in a notable increase in IgG, IgM, interleukins, and cytokines levels, indicating effective antigen clearance over time. In conclusion, our study provides preclinical evidence for designing a highly effective Junin virus vaccine, necessitating further in-vitro and in-vivo experiments.
期刊介绍:
Molecular Diversity is a new publication forum for the rapid publication of refereed papers dedicated to describing the development, application and theory of molecular diversity and combinatorial chemistry in basic and applied research and drug discovery. The journal publishes both short and full papers, perspectives, news and reviews dealing with all aspects of the generation of molecular diversity, application of diversity for screening against alternative targets of all types (biological, biophysical, technological), analysis of results obtained and their application in various scientific disciplines/approaches including:
combinatorial chemistry and parallel synthesis;
small molecule libraries;
microwave synthesis;
flow synthesis;
fluorous synthesis;
diversity oriented synthesis (DOS);
nanoreactors;
click chemistry;
multiplex technologies;
fragment- and ligand-based design;
structure/function/SAR;
computational chemistry and molecular design;
chemoinformatics;
screening techniques and screening interfaces;
analytical and purification methods;
robotics, automation and miniaturization;
targeted libraries;
display libraries;
peptides and peptoids;
proteins;
oligonucleotides;
carbohydrates;
natural diversity;
new methods of library formulation and deconvolution;
directed evolution, origin of life and recombination;
search techniques, landscapes, random chemistry and more;