Evidence map›Paper›PMID 40471879›Full record

ArticlePLoS neglected tropical diseases2025

In silico identification of Leishmania GP63 protein epitopes to generate a new vaccine antigen against leishmaniasis.

Mervenur Güvendi, Hüseyin Can, İrem Yavuz, Ahmet Özbilgin, Aysu Değirmenci Döşkaya, Muhammet Karakavuk, Cemal Ün, Adnan Yüksel Gürüz, İsmail Cem Yılmaz, Mayda Gürsel and 2 more

Abstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors.

Mervenur GüvendiDepartment of Biology Molecular Biology Section, Faculty of Science, Ege University, İzmir, Türkiye.
Hüseyin CanDepartment of Biology Molecular Biology Section, Faculty of Science, Ege University, İzmir, Türkiye.ORCID 0000-0001-9633-9786
İrem YavuzVaccine Development, Application and Research Center, Ege University, İzmir, Türkiye.
Ahmet ÖzbilginDepartment of Parasitology, Faculty of Medicine, Celal Bayar University, Manisa, Türkiye.
Aysu Değirmenci DöşkayaVaccine Development, Application and Research Center, Ege University, İzmir, Türkiye.
Muhammet KarakavukVaccine Development, Application and Research Center, Ege University, İzmir, Türkiye.
Cemal ÜnDepartment of Biology Molecular Biology Section, Faculty of Science, Ege University, İzmir, Türkiye.
Adnan Yüksel GürüzVaccine Development, Application and Research Center, Ege University, İzmir, Türkiye.
İsmail Cem Yılmazİzmir Biomedicine and Genome Center, İzmir, Türkiye.
Mayda Gürselİzmir Biomedicine and Genome Center, İzmir, Türkiye.
İhsan Gürselİzmir Biomedicine and Genome Center, İzmir, Türkiye.
Mert DöşkayaVaccine Development, Application and Research Center, Ege University, İzmir, Türkiye.

Funding

The Scientific and Technological Research Council of Türkiye
6 · The paper itself

Abstract

backgroundThe surface of Leishmania spp. presents glycoprotein 63 (GP63), a metalloprotease that acts as one of the parasite's major antigens. A vaccine against leishmaniasis has not yet been developed and stationary phase promastigotes have utmost importance in transmitting Leishmania spp. from phlebotomine sand fly to humans or reservoirs. Therefore, this study aimed to analyze GP63 protein in three different Leishmania spp. to determine new vaccine candidate antigen against leishmaniasis using sequencing data of locally detected Leishmania strains and in silico approaches. METHODOLOGY/PRINCIPAL

findingsThe GP63 protein sequences of the stationary phase/amastigote form of L. infantum, L. major, and L. tropica were identified and then the gene encoding GP63 protein in Leishmania positive samples (n:59) was amplified and sequenced for variation analysis. According to the results, 4, 6, 19 GP63 variants were found within L. infantum, L. major, and L. tropica isolates, respectively. The most prevalent variants within each species were selected for further analysis using in silico approaches. Accordingly, all selected GP63 proteins were antigenic and the amount of B and T cell epitopes were 23 for L. infantum, 10 for L. major, and 9 for L. tropica. The analysis of each epitope showed that all of them were non-toxic, non-allergen, and soluble but had different antigenicity values. Among these epitopes, EMEDQGSAGSAGS associated with L. major, STHDSGSTTC and AEDILTDEKRDILRK epitopes associated with L. infantum had the highest antigenicity values for B cell, MHC-I, and MHC-II epitopes, respectively. Moreover, conserved epitopes were detected among two or three Leishmania species. CONCLUSIONS/SIGNIFICANCE: This study detected many epitopes that could be used in vaccine studies and the development of serological diagnostic assays.

Indexed as

Antigens, ProtozoanEpitopesLeishmaniaLeishmaniasisLeishmaniasis VaccinesMetalloendopeptidasesComputer SimulationEpitopes, B-LymphocyteEpitopes, T-LymphocyteHumansLeishmania infantumLeishmania majorLeishmania tropicaProtozoan ProteinsAntigens, ProtozoanEpitopesEpitopes, B-LymphocyteEpitopes, T-Lymphocyteglycoprotein gp63, LeishmaniaLeishmaniasis VaccinesMetalloendopeptidasesProtozoan Proteins

Identifiers

PMID40471879
PMCPMC12140206

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.