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Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus

Marburg virus is one of the world’s most threatening diseases, causing extreme hemorrhagic fever, with a death rate of up to 90%. The Food and Drug Administration (FDA) currently not authorized any treatments or vaccinations for the hindrance and post-exposure of the Marburg virus. In the present st...

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Autores principales: Pervin, Tahmina, Oany, Arafat Rahman
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936589/
https://www.ncbi.nlm.nih.gov/pubmed/33717824
http://dx.doi.org/10.1007/s40203-021-00080-3
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author Pervin, Tahmina
Oany, Arafat Rahman
author_facet Pervin, Tahmina
Oany, Arafat Rahman
author_sort Pervin, Tahmina
collection PubMed
description Marburg virus is one of the world’s most threatening diseases, causing extreme hemorrhagic fever, with a death rate of up to 90%. The Food and Drug Administration (FDA) currently not authorized any treatments or vaccinations for the hindrance and post-exposure of the Marburg virus. In the present study, the vaccinomics methodology was adopted to design a potential novel peptide vaccine against the Marburg virus, targeting RNA-directed RNA polymerase (l). A total of 48 l-proteins from diverse variants of the Marburg virus were collected from the NCBI GenBank server and used to classify the best antigenic protein leading to predict equally T and B-cell epitopes. Initially, the top 26 epitopes were evaluated for the attraction with major histocompatibility complex (MHC) class I and II alleles. Finally, four prospective central epitopes NLSDLTFLI, FRYEFTRHF, YRLRNSTAL, and YRVRNVQTL were carefully chosen. Among these, FRYEFTRHF and YRVRNVQTL peptides showed 100% conservancy. Though YRLRNSTAL showed 95.74% conservancy, it demonstrated the highest combined score as T cell epitope (2.5461) and population coverage of 94.42% among the whole world population. The epitope was found non-allergenic, and docking interactions with human leukocyte antigens (HLAs) also verified. Finally, in vivo analysis of the recommended peptides might contribute to the advancement of an efficient and exclusively prevalent vaccine that would be an active route to impede the virus spreading. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s40203-021-00080-3.
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spelling pubmed-79365892021-03-08 Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus Pervin, Tahmina Oany, Arafat Rahman In Silico Pharmacol Original Research Marburg virus is one of the world’s most threatening diseases, causing extreme hemorrhagic fever, with a death rate of up to 90%. The Food and Drug Administration (FDA) currently not authorized any treatments or vaccinations for the hindrance and post-exposure of the Marburg virus. In the present study, the vaccinomics methodology was adopted to design a potential novel peptide vaccine against the Marburg virus, targeting RNA-directed RNA polymerase (l). A total of 48 l-proteins from diverse variants of the Marburg virus were collected from the NCBI GenBank server and used to classify the best antigenic protein leading to predict equally T and B-cell epitopes. Initially, the top 26 epitopes were evaluated for the attraction with major histocompatibility complex (MHC) class I and II alleles. Finally, four prospective central epitopes NLSDLTFLI, FRYEFTRHF, YRLRNSTAL, and YRVRNVQTL were carefully chosen. Among these, FRYEFTRHF and YRVRNVQTL peptides showed 100% conservancy. Though YRLRNSTAL showed 95.74% conservancy, it demonstrated the highest combined score as T cell epitope (2.5461) and population coverage of 94.42% among the whole world population. The epitope was found non-allergenic, and docking interactions with human leukocyte antigens (HLAs) also verified. Finally, in vivo analysis of the recommended peptides might contribute to the advancement of an efficient and exclusively prevalent vaccine that would be an active route to impede the virus spreading. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s40203-021-00080-3. Springer Berlin Heidelberg 2021-03-06 /pmc/articles/PMC7936589/ /pubmed/33717824 http://dx.doi.org/10.1007/s40203-021-00080-3 Text en © The Author(s), under exclusive licence to Springer-Verlag GmbH, DE part of Springer Nature 2021
spellingShingle Original Research
Pervin, Tahmina
Oany, Arafat Rahman
Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title_full Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title_fullStr Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title_full_unstemmed Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title_short Vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of Marburg virus
title_sort vaccinomics approach for scheming potential epitope-based peptide vaccine by targeting l-protein of marburg virus
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936589/
https://www.ncbi.nlm.nih.gov/pubmed/33717824
http://dx.doi.org/10.1007/s40203-021-00080-3
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