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Computational comparison of two new fusion proteins for multiple sclerosis
Multiple sclerosis (MS), as one of the human autoimmune diseases, demyelinates the neurons of the central nervous system (CNS). Activation of the T cells which target the CNS antigens is the first autoimmune event in MS. Myelin oligodendrocyte glycoprotein (MOG) and myelin basic protein (MBP) are tw...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Medknow Publications & Media Pvt Ltd
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6082027/ https://www.ncbi.nlm.nih.gov/pubmed/30271441 http://dx.doi.org/10.4103/1735-5362.236832 |
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author | Payab, Nasrin Mahnam, Karim Shakhsi-Niaei, Mostafa |
author_facet | Payab, Nasrin Mahnam, Karim Shakhsi-Niaei, Mostafa |
author_sort | Payab, Nasrin |
collection | PubMed |
description | Multiple sclerosis (MS), as one of the human autoimmune diseases, demyelinates the neurons of the central nervous system (CNS). Activation of the T cells which target the CNS antigens is the first autoimmune event in MS. Myelin oligodendrocyte glycoprotein (MOG) and myelin basic protein (MBP) are two proteins of the myelin sheath and have been shown to be among the high antigens contributing to the pathogenesis of MS. Production of the drugs with high specificity for the immune system diseases is a concern for various researchers. Therefore, tolerogenic vaccines are considered as a new strategy for the treatment of MS by presenting specific antigens. This study aimed to design and compare two fusion proteins by a combination of two neuroantigens linked to interleukin-16 (IL-16) (MOG-Linker-MBP-IL16 and MBP-Linker-MOG-IL16) as vaccines for MS. In this study, at first two models MOG (aa 11-30) linked to MBP (aa 13-32) was made by Modeler 9.10 and simulated for 20 ns via Gromacs 5.1.1 package. Then simulated antigen domains connected to the N-terminal domain of IL-16 and obtained structures simulated for 50 ns. The results revealed that both constructs had stable structures and the linker could keep two antigenic fragments separate enough, preventing undesired interactions. While MOG-Linker-MBP-IL16 showed better solubility, more accessible surface areas, more flexibility of its IL-16 domain, and better functionality of its IL-16 domain as well as more specific cleavage of its related epitopes after endocytosis lead to a better presentation of its antigenic property. |
format | Online Article Text |
id | pubmed-6082027 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Medknow Publications & Media Pvt Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-60820272018-10-01 Computational comparison of two new fusion proteins for multiple sclerosis Payab, Nasrin Mahnam, Karim Shakhsi-Niaei, Mostafa Res Pharm Sci Original Article Multiple sclerosis (MS), as one of the human autoimmune diseases, demyelinates the neurons of the central nervous system (CNS). Activation of the T cells which target the CNS antigens is the first autoimmune event in MS. Myelin oligodendrocyte glycoprotein (MOG) and myelin basic protein (MBP) are two proteins of the myelin sheath and have been shown to be among the high antigens contributing to the pathogenesis of MS. Production of the drugs with high specificity for the immune system diseases is a concern for various researchers. Therefore, tolerogenic vaccines are considered as a new strategy for the treatment of MS by presenting specific antigens. This study aimed to design and compare two fusion proteins by a combination of two neuroantigens linked to interleukin-16 (IL-16) (MOG-Linker-MBP-IL16 and MBP-Linker-MOG-IL16) as vaccines for MS. In this study, at first two models MOG (aa 11-30) linked to MBP (aa 13-32) was made by Modeler 9.10 and simulated for 20 ns via Gromacs 5.1.1 package. Then simulated antigen domains connected to the N-terminal domain of IL-16 and obtained structures simulated for 50 ns. The results revealed that both constructs had stable structures and the linker could keep two antigenic fragments separate enough, preventing undesired interactions. While MOG-Linker-MBP-IL16 showed better solubility, more accessible surface areas, more flexibility of its IL-16 domain, and better functionality of its IL-16 domain as well as more specific cleavage of its related epitopes after endocytosis lead to a better presentation of its antigenic property. Medknow Publications & Media Pvt Ltd 2018-10 /pmc/articles/PMC6082027/ /pubmed/30271441 http://dx.doi.org/10.4103/1735-5362.236832 Text en Copyright: © 2018 Research in Pharmaceutical Sciences http://creativecommons.org/licenses/by-nc-sa/4.0 This is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 4.0 License, which allows others to remix, tweak, and build upon the work non-commercially, as long as appropriate credit is given and the new creations are licensed under the identical terms. |
spellingShingle | Original Article Payab, Nasrin Mahnam, Karim Shakhsi-Niaei, Mostafa Computational comparison of two new fusion proteins for multiple sclerosis |
title | Computational comparison of two new fusion proteins for multiple sclerosis |
title_full | Computational comparison of two new fusion proteins for multiple sclerosis |
title_fullStr | Computational comparison of two new fusion proteins for multiple sclerosis |
title_full_unstemmed | Computational comparison of two new fusion proteins for multiple sclerosis |
title_short | Computational comparison of two new fusion proteins for multiple sclerosis |
title_sort | computational comparison of two new fusion proteins for multiple sclerosis |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6082027/ https://www.ncbi.nlm.nih.gov/pubmed/30271441 http://dx.doi.org/10.4103/1735-5362.236832 |
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