Comparative proteomic analysis of Leishmania parasites isolated from visceral and cutaneous leishmaniasis patients

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dc.contributor.authorDinç M.
dc.contributor.authorYalçln T.
dc.contributor.authorÇavuş I.
dc.contributor.authorÖzbilgin A.
dc.date.accessioned2024-07-22T08:04:47Z
dc.date.available2024-07-22T08:04:47Z
dc.date.issued2022
dc.description.abstractLeishmaniasis is an infectious disease in which different clinical manifestations are classified into three primary forms: visceral, cutaneous and mucocutaneous. These disease forms are associated with parasite species of the protozoan genus Leishmania. For instance, Leishmania infantum and Leishmania tropica are typically linked with visceral (VL) and cutaneous (CL) leishmaniasis, respectively; however, these two species can also cause other form to a lesser extent. What is more alarming is this characteristic, which threatens current medical diagnosis and treatment, is started to be acquired by other species. Our purpose was to address this issue; therefore, gel-based and gel-free proteomic analyses were carried out on the species L. infantum to determine the proteins differentiating between the parasites caused VL and CL. In addition, L. tropica parasites representing the typical cases for CL were included. According to our results, electrophoresis gels of parasites caused to VL were distinguishable regarding the repetitive down-regulation on some specific locations. In addition, a distinct spot of an antioxidant enzyme, superoxide dismutase, was shown up only on the gels of CL samples regardless of the species. In the gel-free approach, 37 proteins that were verified with a second database search using a different search engine, were recognized from the comparison between VL and CL samples. Among them, 31 proteins for the CL group and six proteins for the VL group were determined differentially abundant. Two proteins from the gel-based analysis, pyruvate kinase and succinyl-coA:3-ketoacid-coenzyme A transferase analysis were encountered in the protein list of the CL group. Copyright © The Author(s), 2021. Published by Cambridge University Press.
dc.identifier.DOI-ID10.1017/S0031182021001967
dc.identifier.issn00311820
dc.identifier.urihttp://akademikarsiv.cbu.edu.tr:4000/handle/123456789/12848
dc.language.isoEnglish
dc.publisherCambridge University Press
dc.rightsAll Open Access; Green Open Access
dc.subjectAnimals
dc.subjectHumans
dc.subjectLeishmania infantum
dc.subjectLeishmania tropica
dc.subjectLeishmaniasis, Cutaneous
dc.subjectLeishmaniasis, Visceral
dc.subjectParasites
dc.subjectProteomics
dc.subject3 oxoacid coenzyme A transferase
dc.subjectadenosine triphosphatase
dc.subjectaminopeptidase
dc.subjectantioxidant
dc.subjectarsenical pump driving atpase homolog
dc.subjectaspartate aminotransferase
dc.subjectautoantigen
dc.subjectbeta eliminating lyase
dc.subjectcarboxypeptidase
dc.subjectcarrier protein
dc.subjectcoproporphyrinogen oxidase
dc.subjectdihydrolipoamide dehydrogenase
dc.subjectdipeptidyl carboxypeptidase
dc.subjecteukaryotic release factor 3
dc.subjectflavine mononucleotide transferase
dc.subjectflavoprotein
dc.subjectflavoprotein subunit like protein
dc.subjectfumarate hydratase
dc.subjectglucosyltransferase
dc.subjectglutamamyl carboxypeptidase
dc.subjectglutamate ammonia ligase
dc.subjectglutamine fructose 6 phosphate aminotransferase
dc.subjectglycosomal membrane protein
dc.subjectguanine nucleotide binding protein
dc.subjectheat shock protein 70
dc.subjecthydrolase
dc.subjectI 6 autoantigen like protein
dc.subjectI 6 autoantigen-like protein
dc.subjectinitiation factor 4A
dc.subjectisomerase
dc.subjectlevo glutamate gamma semialdehyde dehydrogenase
dc.subjectlyase
dc.subjectmalate dehydrogenase
dc.subjectmembrane protein
dc.subjectmetal ion transporter
dc.subjectmetalloproteinase
dc.subjectmethyl 5' thioadenosine phosphorylase
dc.subjectmevalonate kinase
dc.subjectMORN repeat protein
dc.subjectn acyl amino acid amidohydrolase
dc.subjectn ethylmaleimide sensitive factor
dc.subjectoxidoreductase
dc.subjectperoxidoxin
dc.subjectphosphorylase
dc.subjectproline dehydrogenase
dc.subjectprotozoal protein
dc.subjectpyruvate kinase
dc.subjectribonucleoside diphosphate reductase
dc.subjectRNA recognition motif protein
dc.subjectserine transfer RNA ligase
dc.subjectsterol 14alpha demethylase
dc.subjectsuperoxide dismutase
dc.subjectsurf1 like protein
dc.subjecttransferase
dc.subjectunclassified drug
dc.subjecturidine diphosphate glucose glucosyltransferase
dc.subjectzinc finger protein
dc.subjectArticle
dc.subjectbioinformatics
dc.subjectcontrolled study
dc.subjectcutaneous leishmaniasis
dc.subjectdifferential gene expression
dc.subjectdown regulation
dc.subjectgene location
dc.subjecthuman
dc.subjectLeishmania infantum
dc.subjectLeishmania tropica
dc.subjectmolecular weight
dc.subjectnonhuman
dc.subjectpeptide mass fingerprinting
dc.subjectpH
dc.subjectpolyacrylamide gel electrophoresis
dc.subjectpromastigote
dc.subjectprotein database
dc.subjectprotein expression level
dc.subjectproteomics
dc.subjectsearch engine
dc.subjectshotgun sequencing
dc.subjecttime of flight mass spectrometry
dc.subjecttwo dimensional gel electrophoresis
dc.subjectvisceral leishmaniasis
dc.subjectanimal
dc.subjectcutaneous leishmaniasis
dc.subjectparasite
dc.subjectparasitology
dc.subjectproteomics
dc.subjectvisceral leishmaniasis
dc.titleComparative proteomic analysis of Leishmania parasites isolated from visceral and cutaneous leishmaniasis patients
dc.typeArticle

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