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Methicillin-resistant (MRSA) is an opportunistic pathogen and responsible for causing life-threatening infections. The emergence of hypervirulent and multidrug-resistant (MDR) strains led to challenging issues in antibiotic therapy. Consequently, the morbidity and mortality rates caused by infections have a substantial impact on health concerns. The current worldwide prevalence of MRSA infections highlights the need for long-lasting preventive measures and strategies. Unfortunately, effective measures are limited. In this study, we focus on the identification of vaccine candidates and drug target proteins against the 16 strains of MRSA using reverse vaccinology and subtractive genomics approaches. Using the reverse vaccinology approach, 4 putative antigenic proteins were identified; among these, PrsA and EssA proteins were found to be more promising vaccine candidates. We applied a molecular docking approach of selected 8 drug target proteins with the drug-like molecules, revealing that the ZINC4235426 as potential drug molecule with favorable interactions with the target active site residues of 5 drug target proteins , biotin protein ligase, HPr kinase/phosphorylase, thymidylate kinase, UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase, and pantothenate synthetase. Thus, the identified proteins can be used for further rational drug or vaccine design to identify novel therapeutic agents for the treatment of multidrug-resistant staphylococcal infection.
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http://dx.doi.org/10.3390/molecules27072083 | DOI Listing |
Mol Genet Genomics
September 2025
Department of Biochemistry, Bahauddin Zakariya University, Multan, Multan, 66000, Punjab, Pakistan.
Moraxella catarrhalis is a Gram-negative diplococcus bacterium and a common respiratory pathogen, implicated in 15-20% of otitis media (OM) cases in children and chronic obstructive pulmonary disease (COPD) in adults. The rise of drug-resistant Moraxella catarrhalis has highlighted the urgent need for the potent vaccine strategies to reduce its clinical burden. Despite a mortality rate of 13%, there is no FDA-approved vaccine for this pathogen.
View Article and Find Full Text PDFComput Biol Med
September 2025
Structural Biology and Bio-Computing Lab, Department of Bioinformatics, Science Block, Alagappa University, Karaikudi, 630 003, Tamil Nadu, India. Electronic address:
Antimicrobial resistance endangers global health by rapidly disseminating Multidrug-resistant (MDR) pathogens that undermine antibiotic therapies. P.aeruginosa, a high-priority ESKAPE pathogen, exemplifies the crisis with complex resistance mechanisms that demand alternative strategies beyond conventional antibiotics.
View Article and Find Full Text PDFBiology (Basel)
August 2025
Lab of Biological Chemistry, School of Medicine, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece.
Background: Multi-epitope vaccines have become the preferred strategy for protection against infectious diseases by integrating multiple MHC-restricted T-cell and B-cell epitopes that elicit both humoral and cellular immune responses against pathogens. Computational methods address various aspects independently, yet their orchestration is technically challenging, as most bioinformatics tools are accessible through heterogeneous interfaces and lack interoperability features. The present work proposes a novel framework for rationalized multi-epitope vaccine design that streamlines end-to-end analyses through an integrated web-based environment.
View Article and Find Full Text PDFSci Rep
September 2025
Department of Basic Health Sciences, College of Applied Medical Sciences, Qassim University, Buraydah, Saudi Arabia.
Salmonella enterica subsp. enterica serotype Typhi (Salmonella typhi) is the cause of typhoid fever, a severe public health issue in impoverished countries with inadequate sanitation. Despite the availability of therapies, infection rates remain high, underscoring the critical need for an effective and long-lasting vaccine.
View Article and Find Full Text PDFACS Infect Dis
August 2025
Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri 63130-4899, United States.
Next-generation tetracycline antibiotics are threatened by an emerging resistance mechanism ─ enzymatic inactivation. The relevant enzymes ─ tetracycline destructases (TDases) ─ are structural homologues of class A flavin monooxygenase (FMO) that oxidize tetracycline antibiotics, leading to various inactive degradation products. Small molecule inhibitors of antibiotic-inactivating enzymes are critical clinical therapeutics used to manage bacterial resistance with combination therapy.
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