Evidence map›Paper›PMID 40768028›Full record

ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2025

Immunoinformatics analysis of the proteins MPT83 and MPT51 to design a possible chimeric vaccine against Mycobacterium tuberculosis.

Rebeca Trícia Oliveira Loureiro, Sara Jessica Teixeira Andrade, Edson Junior do Carmo, André Miasato Higa, Rudi Emerson de Lima Procópio

Abstract read
In one paragraph

Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 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. Drug resistance mechanisms inFrontiers in pharmacology · 2026
    Review
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

5 authors.

Rebeca Trícia Oliveira LoureiroUniversidade do Estado do Amazonas, Programa de Pós-Graduação em Biotecnologia e Recursos Naturais da Amazônia, Manaus, AM, Brazil. rebecatriciaol@gmail.com.
Sara Jessica Teixeira AndradeUniversidade do Estado do Amazonas, Programa de Pós-Graduação em Biotecnologia e Recursos Naturais da Amazônia, Manaus, AM, Brazil.
Edson Junior do CarmoInstituto de Ciências Biológicas, Programa de Pós-Graduação em Biotecnologia, Universidade Federal do Amazonas, Manaus, AM, Brazil.
André Miasato HigaUniversidade do Estado do Amazonas, Programa de Pós-Graduação em Biotecnologia e Recursos Naturais da Amazônia, Manaus, AM, Brazil.
Rudi Emerson de Lima ProcópioUniversidade do Estado do Amazonas, Programa de Pós-Graduação em Biotecnologia e Recursos Naturais da Amazônia, Manaus, AM, Brazil.

Funding

Fapeam Fapeam
6 · The paper itself

Abstract

Mycobacterium tuberculosis (Mtb) is the pathogen that causes tuberculosis (TB). This disease affects one-third of the world's population, mainly in its latent form. The use of reverse vaccinology and immunoinformatics stands out for the production of vaccines based on peptides or proteins, since they are more specific, safe, effective and economical. The present study evaluated the immunological potential of the proteins MPT83 and MPT51 for vaccine production, comparing them with MPT64. To do this, the sequences of these proteins from MTB H37Rv were downloaded and analyzed. The prediction of T and B cell epitopes was performed, and the adjuvant (50 S L7/L12) was included in the fusion of MPT83 and MPT51 to enhance the immune response. The allergenicity, antigenicity, solubility and physicochemical properties of the fused protein fragments were evaluated. Through different programs, a variety of bioinformatics tools were used to predict, analyze and validate the tertiary structure. The results of the in silico immunological simulation of the chimeric protein demonstrated that the best region for use as an epitope is the initial part of MPT83, consisting of 100 amino acid residues, and the final portion of MPT51, consisting of 99 amino acid residues, with a significant immunological response, excellent antigenicity (1.02) and no allergenicity. The secondary structure revealed that the majority of alpha-helices are in the initial part of the proteins, and the chimeric vaccine has 3 beta strands along its length. Finally, the chimeric vaccine candidate and MPT64 were efficiently cloned into the bacterial vector and successfully expressed in Escherichia coli thereby facilitating future in vivo studies with potentially promising results.

Indexed as

Antigens, BacterialBacterial ProteinsMycobacterium tuberculosisTuberculosisTuberculosis VaccinesComputational BiologyEpitopes, B-LymphocyteEpitopes, T-LymphocyteHumansImmunoinformaticsRecombinant Fusion ProteinsAntigens, BacterialBacterial ProteinsEpitopes, B-LymphocyteEpitopes, T-LymphocyteMPT51 protein, MycobacteriumRecombinant Fusion ProteinsTuberculosis VaccinesAntigenEpitopeMPT proteinMycobacterium tuberculosisVaccine

Identifiers

PMID40768028
PMCPMC12660520

What Socratic holds

Textmetadata
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Registered trials

None linked

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 Socratic graph.