ArticleCurrent topics in medicinal chemistry2025
Superbug
Article in Current topics in medicinal chemistry, 2025. 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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Abstract
introductionNeisseria gonorrhoeae is a notorious superbug responsible for causing 'Gonorrhoea' in humans. Recently, it has been classified as a high-priority pathogen by the World Health Organization due to its increasing resistance to available antibiotics. A multi-prolonged approach is needed to combat the growing problem of drug resistance caused by N. gonorrhoeae. This study evaluates Glutamate Racemase (GR), a moonlight protein of N. gonorrhoeae (Ng-GR), as a novel therapeutic target with potential for both inhibitor design and peptide vaccine development. Ng-GR plays a crucial role in the peptidoglycan biosynthetic pathway and is highly conserved across bacterial species. Additionally, this protein moonlights to perform a secondary function by binding to DNA gyrase in various organisms.
methodsHomology modeling, molecular docking, and molecular dynamics simulations were used to design inhibitors targeting the moonlight function of Ng-GR. The immunogenicity of this protein was assessed using ABCPred-2.0, BepiPred-2.0, and ProPred softwares.
resultsBisleucocurine A was found to bind at the ectopic site of Ng-GR, disrupting its crucial moonlight function and interfering its interaction with N. gonorroheae DNA Gyrase (Ng-gyrase). Interestingly, residues important for its moonlight function were also identified as key immunogenic sites using ABCPred-2.0, BepiPred-2.0, and ProPred softwares, enhancing the potential of this protein as a vaccine candidate.
conclusionThe GR enzyme's moonlight function is highlighted as a promising novel target for therapeutic intervention and vaccine development in N. gonorrohoeae.
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