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A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis
BACKGROUND: Leishmania is a mandatory intracellular pathogen and causing neglected disease. Hence, protection against leishmaniasis by a development vaccine is an important subject. This study aimed to design a poly-epitope vaccine for cutaneous leishmaniasis. METHODS: The present study was conducte...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Tehran University of Medical Sciences
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8418661/ https://www.ncbi.nlm.nih.gov/pubmed/34557233 http://dx.doi.org/10.18502/ijpa.v16i2.6267 |
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author | Ahmadpour, Niloofar Bavarsad Dalimi, Abdolhossein Pirestani, Majid Sadraei, Javid |
author_facet | Ahmadpour, Niloofar Bavarsad Dalimi, Abdolhossein Pirestani, Majid Sadraei, Javid |
author_sort | Ahmadpour, Niloofar Bavarsad |
collection | PubMed |
description | BACKGROUND: Leishmania is a mandatory intracellular pathogen and causing neglected disease. Hence, protection against leishmaniasis by a development vaccine is an important subject. This study aimed to design a poly-epitope vaccine for cutaneous leishmaniasis. METHODS: The present study was conducted in the Parasitology Department of Tarbiat Modares University, Tehran, Iran during 2017–2019. Several bioinformatics methods at online servers were used for prediction of different aspects of poly-epitope, including, physico-chemical attributes, allergenicity, antigenicity, secondary and tertiary structures, B-cell, T-cell and MHC (I, II) potential epitopes of LACK, LEIF, GP63 and SMT antigens of L. major. RESULTS: After designing the construct (GLSL), the outputs of PTM sites demonstrated that the poly-epitope had 57 potential sites for phosphorylation. Furthermore, the secondary of GLSL structure includes 59.42%, 20.94% and 19.63% for random coil, extended strand and alpha-helix, respectively. The GLSL is an immunogenic protein with an acceptable antigenicity (0.8410) and non-allergen. Afterward, 20 potential epitopes of LACK, LEIF, GP63 and SMT antigens were linked by a flexible linker (SAPGTP), then was synthesized, and sub-cloned in pLEXY– neo2. The results were confirmed the expression of 38.7 kDa poly-epitope in secretory and cytosolic sites, separately. CONCLUSION: A good expression in the L. tarentulae and confirmation of the GLSL poly-epitope could be a basis for developing a vaccine candidate against leishmaniasis that should be confirmed via experimental tests in BALB/c mice. |
format | Online Article Text |
id | pubmed-8418661 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Tehran University of Medical Sciences |
record_format | MEDLINE/PubMed |
spelling | pubmed-84186612021-09-22 A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis Ahmadpour, Niloofar Bavarsad Dalimi, Abdolhossein Pirestani, Majid Sadraei, Javid Iran J Parasitol Original Article BACKGROUND: Leishmania is a mandatory intracellular pathogen and causing neglected disease. Hence, protection against leishmaniasis by a development vaccine is an important subject. This study aimed to design a poly-epitope vaccine for cutaneous leishmaniasis. METHODS: The present study was conducted in the Parasitology Department of Tarbiat Modares University, Tehran, Iran during 2017–2019. Several bioinformatics methods at online servers were used for prediction of different aspects of poly-epitope, including, physico-chemical attributes, allergenicity, antigenicity, secondary and tertiary structures, B-cell, T-cell and MHC (I, II) potential epitopes of LACK, LEIF, GP63 and SMT antigens of L. major. RESULTS: After designing the construct (GLSL), the outputs of PTM sites demonstrated that the poly-epitope had 57 potential sites for phosphorylation. Furthermore, the secondary of GLSL structure includes 59.42%, 20.94% and 19.63% for random coil, extended strand and alpha-helix, respectively. The GLSL is an immunogenic protein with an acceptable antigenicity (0.8410) and non-allergen. Afterward, 20 potential epitopes of LACK, LEIF, GP63 and SMT antigens were linked by a flexible linker (SAPGTP), then was synthesized, and sub-cloned in pLEXY– neo2. The results were confirmed the expression of 38.7 kDa poly-epitope in secretory and cytosolic sites, separately. CONCLUSION: A good expression in the L. tarentulae and confirmation of the GLSL poly-epitope could be a basis for developing a vaccine candidate against leishmaniasis that should be confirmed via experimental tests in BALB/c mice. Tehran University of Medical Sciences 2021 /pmc/articles/PMC8418661/ /pubmed/34557233 http://dx.doi.org/10.18502/ijpa.v16i2.6267 Text en Copyright © 2021 Bavarsad Ahmadpour et al. Published by Tehran University of Medical Sciences https://creativecommons.org/licenses/by-nc/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International license (https://creativecommons.org/licenses/by-nc/4.0/). Non-commercial uses of the work are permitted, provided the original work is properly cited. |
spellingShingle | Original Article Ahmadpour, Niloofar Bavarsad Dalimi, Abdolhossein Pirestani, Majid Sadraei, Javid A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title | A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title_full | A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title_fullStr | A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title_full_unstemmed | A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title_short | A Novel Chimeric Antigen as a Vaccine Candidate against Leishmania major: In silico Analysis |
title_sort | novel chimeric antigen as a vaccine candidate against leishmania major: in silico analysis |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8418661/ https://www.ncbi.nlm.nih.gov/pubmed/34557233 http://dx.doi.org/10.18502/ijpa.v16i2.6267 |
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