نمایش مختصر رکورد

dc.contributor.authorMotamedpour, Leilaen_US
dc.contributor.authorDalimi, Abdolhosseinen_US
dc.contributor.authorPirestani, Majiden_US
dc.contributor.authorGhafarifar, Fatemehen_US
dc.date.accessioned1399-07-09T08:25:50Zfa_IR
dc.date.accessioned2020-09-30T08:25:50Z
dc.date.available1399-07-09T08:25:50Zfa_IR
dc.date.available2020-09-30T08:25:50Z
dc.date.issued2020-11-01en_US
dc.date.issued1399-08-11fa_IR
dc.date.submitted2019-12-28en_US
dc.date.submitted1398-10-07fa_IR
dc.identifier.citationMotamedpour, Leila, Dalimi, Abdolhossein, Pirestani, Majid, Ghafarifar, Fatemeh. (2020). <i>In silico</i> analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasis. Iranian Journal of Basic Medical Sciences, 23(11), 1409-1418. doi: 10.22038/ijbms.2020.45394.10561en_US
dc.identifier.issn2008-3866
dc.identifier.issn2008-3874
dc.identifier.urihttps://dx.doi.org/10.22038/ijbms.2020.45394.10561
dc.identifier.urihttp://ijbms.mums.ac.ir/article_16432.html
dc.identifier.urihttps://iranjournals.nlai.ir/handle/123456789/341248
dc.description.abstract<em><strong>Objective(s):</strong></em> 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.<br /><em><strong>Materials and Methods:</strong></em> 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.<br /><em><strong>Results:</strong></em> 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. <br /><em><strong>Conclusion:</strong></em> 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.en_US
dc.format.extent1083
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoen_US
dc.publisherMashhad University of Medical Sciencesen_US
dc.relation.ispartofIranian Journal of Basic Medical Sciencesen_US
dc.relation.isversionofhttps://dx.doi.org/10.22038/ijbms.2020.45394.10561
dc.subjectBioinformaticsen_US
dc.subjectLeishmania majoren_US
dc.subjectPolytopeen_US
dc.subjectTLGLen_US
dc.subjectVaccineen_US
dc.title<i>In silico</i> analysis and expression of a new chimeric antigen as a vaccine candidate against cutaneous leishmaniasisen_US
dc.typeTexten_US
dc.typeOriginal Articleen_US
dc.contributor.departmentParasitology Department, Medical Sciences Faculty, Tarbiat Modares University, Tehran, Iranen_US
dc.contributor.departmentParasitology Department, Medical Sciences Faculty, Tarbiat Modares University, Tehran, Iranen_US
dc.contributor.departmentParasitology Department, Medical Sciences Faculty, Tarbiat Modares University, Tehran, Iranen_US
dc.contributor.departmentParasitology Department, Medical Sciences Faculty, Tarbiat Modares University, Tehran, Iranen_US
dc.citation.volume23
dc.citation.issue11
dc.citation.spage1409
dc.citation.epage1418
nlai.contributor.orcid0000000340610754
nlai.contributor.orcid0000-0001-5591-5513
nlai.contributor.orcid0000-0003-0891-8214


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