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In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis

OBJECTIVE(S): Since leishmaniasis is one of the health problems in many countries, the development of preventive vaccines against it is a top priority. Peptide vaccines may be a new way to fight the Leishmania infection. In this study, a silicon method was used to predict and analyze B and T cells t...

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Autores principales: Motamedpour, Leila, Dalimi, Abdolhossein, Pirestani, Majid, Ghaffarifar, Fatemeh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Mashhad University of Medical Sciences 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7671421/
https://www.ncbi.nlm.nih.gov/pubmed/33235698
http://dx.doi.org/10.22038/ijbms.2020.45394.10561
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author Motamedpour, Leila
Dalimi, Abdolhossein
Pirestani, Majid
Ghaffarifar, Fatemeh
author_facet Motamedpour, Leila
Dalimi, Abdolhossein
Pirestani, Majid
Ghaffarifar, Fatemeh
author_sort Motamedpour, Leila
collection PubMed
description OBJECTIVE(S): Since leishmaniasis is one of the health problems in many countries, the development of preventive vaccines against it is a top priority. Peptide vaccines may be a new way to fight the Leishmania infection. In this study, a silicon method was used to predict and analyze B and T cells to produce a vaccine against cutaneous leishmaniasis. MATERIALS AND METHODS: Immunodominant epitope of Leishmania were selected from four TSA, LPG3, GP63, and Lmsti1 antigens and linked together using a flexible linker (SAPGTP). The antigenic and allergenic features, 2D and 3D structures, and physicochemical features of a chimeric protein were predicted. Finally, through bioinformatics methods, the mRNA structure was predicted and was produced chemically and cloned into the pLEXY-neo2 vector. RESULTS: Results indicated, polytope had no allergenic properties, but its antigenicity was estimated to be 0.92%. The amino acids numbers, molecular weight as well as negative and positive charge residuals were estimated 390, ~41KDa, 41, and 30, respectively. The results showed that the designed polytope has 50 post-translationally modified sites. Also, the secondary structure of the protein is composed of 25.38% alpha-helix, 12.31% extended strand, and 62.31% random coil. The results of SDS-PAGE and Western blotting revealed the recombinant protein with ~ 41 kDa. The results of Ramachandran plot showed that 96%, 2.7%, and 1.3% of amino acid residues were located in the preferred, permitted, and outlier areas, respectively. CONCLUSION: It is expected that the TLGL polytope will produce a cellular immune response. Therefore, the polytope could be a good candidate for an anti-leishmanial vaccine.
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spelling pubmed-76714212020-11-23 In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis Motamedpour, Leila Dalimi, Abdolhossein Pirestani, Majid Ghaffarifar, Fatemeh Iran J Basic Med Sci Original Article OBJECTIVE(S): Since leishmaniasis is one of the health problems in many countries, the development of preventive vaccines against it is a top priority. Peptide vaccines may be a new way to fight the Leishmania infection. In this study, a silicon method was used to predict and analyze B and T cells to produce a vaccine against cutaneous leishmaniasis. MATERIALS AND METHODS: Immunodominant epitope of Leishmania were selected from four TSA, LPG3, GP63, and Lmsti1 antigens and linked together using a flexible linker (SAPGTP). The antigenic and allergenic features, 2D and 3D structures, and physicochemical features of a chimeric protein were predicted. Finally, through bioinformatics methods, the mRNA structure was predicted and was produced chemically and cloned into the pLEXY-neo2 vector. RESULTS: Results indicated, polytope had no allergenic properties, but its antigenicity was estimated to be 0.92%. The amino acids numbers, molecular weight as well as negative and positive charge residuals were estimated 390, ~41KDa, 41, and 30, respectively. The results showed that the designed polytope has 50 post-translationally modified sites. Also, the secondary structure of the protein is composed of 25.38% alpha-helix, 12.31% extended strand, and 62.31% random coil. The results of SDS-PAGE and Western blotting revealed the recombinant protein with ~ 41 kDa. The results of Ramachandran plot showed that 96%, 2.7%, and 1.3% of amino acid residues were located in the preferred, permitted, and outlier areas, respectively. CONCLUSION: It is expected that the TLGL polytope will produce a cellular immune response. Therefore, the polytope could be a good candidate for an anti-leishmanial vaccine. Mashhad University of Medical Sciences 2020-11 /pmc/articles/PMC7671421/ /pubmed/33235698 http://dx.doi.org/10.22038/ijbms.2020.45394.10561 Text en This is an Open Access article distributed under the terms of the Creative Commons Attribution License, (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Motamedpour, Leila
Dalimi, Abdolhossein
Pirestani, Majid
Ghaffarifar, Fatemeh
In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title_full In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title_fullStr In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title_full_unstemmed In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title_short In silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
title_sort in silico analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7671421/
https://www.ncbi.nlm.nih.gov/pubmed/33235698
http://dx.doi.org/10.22038/ijbms.2020.45394.10561
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