Evidence map›Paper›PMID 42101130›Full record

ArticleBiotechnology and applied biochemistry2026

Immunoinformatics-Based Design of a Multi-Epitope Vaccine Targeting a Conserved Copper-Associated Protein in Neisseria gonorrhoeae.

Sinethemba H Yakobi, Uchechukwu U Nwodo

Abstract read
In one paragraph

Article in Biotechnology and applied biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Sinethemba H YakobiPatho-Biocatalysis Group (PBG), Department of Biochemistry and Biological Sciences, University of Fort Hare, Alice, South Africa.
Uchechukwu U NwodoPatho-Biocatalysis Group (PBG), Department of Biochemistry and Biological Sciences, University of Fort Hare, Alice, South Africa.

Funding

Department of Science and Innovation and the Technology Innovation Agency
6 · The paper itself

Abstract

Neisseria gonorrhoeae poses an urgent public health challenge due to rapidly increasing antimicrobial resistance and the absence of an effective vaccine. Targeting conserved bacterial pathways involved in essential physiological processes may provide new opportunities for vaccine antigen discovery. In this study, we applied an immunoinformatics-based pipeline to explore a conserved copper-associated protein as a potential antigenic source for multi-epitope vaccine design. Analysis of 396 clinical genomes confirmed high assembly quality and identified a highly conserved hypothetical protein (AKOBGLPP_01618) through proteome-wide screening for metal-binding signatures. The candidate exhibited strong predicted antigenicity, high prevalence across isolates (99.5%), and no detectable homology with human proteins. In silico analyses suggested potential copper-binding features based on predicted metal-coordinating residues and conserved genomic context. Epitope mapping identified B-cell epitope-rich regions that were refined into conserved, surface-accessible peptides. Predicted cytotoxic and helper T-cell epitopes were filtered for immunogenicity, safety, and strain conservancy prior to inclusion in a multi-epitope construct containing a TLR4-targeting adjuvant and processing-optimized linkers. The resulting 155-amino-acid construct demonstrated favorable physicochemical characteristics, predicted solubility, and an estimated global population coverage of 74.84%. Docking analyses suggested a consistent interaction propensity with the TLR4/MD-2 complex across multiple predicted conformations. Although these findings provide preliminary computational support for the proposed construct, experimental validation will be required to confirm antigen function, immunogenicity, and receptor engagement. Collectively, this study identifies a conserved copper-associated protein as a potential antigen source and presents a computational framework for exploring vaccine candidates against N. gonorrhoeae.

Indexed as

Bacterial ProteinsBacterial VaccinesCopperEpitopesNeisseria gonorrhoeaeEpitopes, B-LymphocyteHumansImmunoinformaticsProtein Subunit VaccinesBacterial ProteinsBacterial VaccinesCopperEpitopesEpitopes, B-LymphocyteProtein Subunit Vaccinesconserved antigencopper homeostasisepitope predictionimmunoinformaticsmulti‐epitope vaccineNeisseria gonorrhoeae

Identifiers

PMID42101130
PMCPMC13644377

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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.