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<p><i>Staphylococcus epidermidis</i> is a major component of the skin flora. This common inhabitant of the human skin is actually considered as an important opportunistic pathogens and a leading cause of hospital acquired infections. The aim of the present study was to predict B cell and T cell epitopes from different virulent proteins sequences to design a potential multi-epitope vaccine against this multidrug resistant bacterium. Twelve proteins which are involved in the virulence of <i>Staphylococcus epidermidis</i>, were subjected to an <i>in silico</i> reverse vaccinology approach. The three-dimensional structure of the vaccine construct was predicted, and its quality was evaluated. Protein- protein docking and flexibility analysis were then performed. An <i>in silico</i> cloning and a computational immune simulation analysis were also carried out to validate this multi-epitopes fusion. The results reveal that the developed vaccine has a good binding affinity and high stability in complex with the TLR8 receptor (binding energy values ranging from—9.8 to -15.8&#xa0;kcal/mol) as well as efficient expression in&#xa0;<i>Escherichia coli</i>&#xa0;(CAI 0.97; GC content 49.64%) and effective immune response against <i>Staphylococcus epidermidis.</i> These theoretical results show that the twelve virulent proteins could be used to create a new, potent vaccine against <i>Staphylococcus epidermidis.</i> Further experimental studies are essential to validate the efficacy and safety of this multiepitope vaccine candidate.</p>

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Structural exploration of Staphylococcus epidermidis virulence proteins for multi-epitope vaccine peptide design

  • 期刊论文

  • 发表日期：

    2025年12月4日

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  • Nora Laref,
  • Khadidja Belkheir

摘要

Staphylococcus epidermidis is a major component of the skin flora. This common inhabitant of the human skin is actually considered as an important opportunistic pathogens and a leading cause of hospital acquired infections. The aim of the present study was to predict B cell and T cell epitopes from different virulent proteins sequences to design a potential multi-epitope vaccine against this multidrug resistant bacterium. Twelve proteins which are involved in the virulence of Staphylococcus epidermidis, were subjected to an in silico reverse vaccinology approach. The three-dimensional structure of the vaccine construct was predicted, and its quality was evaluated. Protein- protein docking and flexibility analysis were then performed. An in silico cloning and a computational immune simulation analysis were also carried out to validate this multi-epitopes fusion. The results reveal that the developed vaccine has a good binding affinity and high stability in complex with the TLR8 receptor (binding energy values ranging from—9.8 to -15.8 kcal/mol) as well as efficient expression in Escherichia coli (CAI 0.97; GC content 49.64%) and effective immune response against Staphylococcus epidermidis. These theoretical results show that the twelve virulent proteins could be used to create a new, potent vaccine against Staphylococcus epidermidis. Further experimental studies are essential to validate the efficacy and safety of this multiepitope vaccine candidate.