ArticleAmino acids2026
Computational identification of antigens and development of a multi-epitope vaccine for bacterial vaginosis caused by Gardnerella vaginalis.
Article in Amino acids, 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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Abstract
Bacterial vaginosis (BV), a prevalent form of vaginal dysbiosis, is primarily caused by Gardnerella vaginalis. The increasing prevalence of BV has raised global health concerns, prompting the need for a vaccine that can enhance human immunity and mitigate BV transmission. The study developed a multi-epitope vaccine for BV infection using immunoinformatic methodologies. B-cell and T-cell epitopes were identified using the IEDB recommended server and NetCTL. Specifically, HTL epitopes were predicted against HLA-DR alleles (including DRB101:01, DRB103:05, and DRB104:04), while CTL epitopes were predicted against HLA class I supertypes (including HLA-A02:01 and HLA-A*01:01). The selected epitopes were fused using adjuvants and linkers. The peptide sequence MSPSVRHSPSVRH, derived from the heat shock protein 60 (HSP60) of Mycobacterium tuberculosis, was incorporated as an adjuvant to activate innate immunity via TLR2/4 and enhance dendritic cell maturation. The B-cell and (CTL or HTL) epitopes were connected using GGGS linkers, whereas the CTL + HTL epitopes were connected using HEYGAEALERAG linkers. Additional epitopes were chosen based on antigenicity, allergenicity, and immunological features. TLR2 recognizes bacterial lipoproteins and peptidoglycan. TLR2 and TLR-4 showed robust interactions in molecular docking. The results of the present study demonstrate that the produced vaccine displayed stability, shown by a molecular weight of 49924.79 Da and an antigenicity value of 1.37. The Vaccine Construct demonstrated stability and basicity, shown by an instability score of 32.65 and a projected isoelectric point (pI) of 5.09. The expected secondary structure of the vaccine construct consisted of 94.57% random coil, and 5.43% extended strand. The suggested vaccine demonstrated efficient binding to its TLR2 and TLR4 receptors, yielding the maximum Van der Waals energy of (-97.2 +/- 5.9) and (-67.6 +/- 7.3) kcal/mol, respectively. The polypeptide vaccine's stability and compactness were assessed using molecular dynamics simulations. The vaccine showed favorable stability, expression, immunostimulatory properties, and solubility.
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