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<p>Leptospirosis is a globally neglected zoonotic disease caused by the spirochete <i>Leptospira interrogans</i>, posing a major public health burden in tropical and subtropical regions. Although antibiotic therapy remains the primary treatment for most bacterial infections, <i>L. interrogans</i> has exhibited increasing resistance to antimicrobial agents, underscoring the need for alternative prophylactic strategies and prompting further research into B-cell peptide epitope-based vaccines as a long-term solution for disease control. This study explored the outer membrane proteins LIC11574 and LIC13411 as sources of B-cell epitopes for rational vaccine development. Using bioinformatics and immune simulations, candidate epitopes were identified based on antigenicity, non-allergenicity, and immunogenicity. A total of 69 16-mer and 68 18-mer epitopes were identified in LIC11574, while LIC13411 yielded 112 16-mer and 123 18-mer epitopes. Structural investigation revealed that the identified B-cell peptide epitopes were predominantly located within α-helical regions, whereas the remaining sequences were distributed across β-sheet structures and loop regions. The top-ranked B-cell peptide epitopes of LIC11574 and LIC13411, selected for their antigenic and non-allergenic characteristics, were successfully docked with the HLA-DRB1*15 molecule, exhibiting promising binding affinities ranging from − 12.6 to −&#xa0;14.9&#xa0;kcal/mol. Immune simulations also revealed that the constructed multi-epitope vaccines induced B-cell and helper T-cell activities, indicating a favorable host immune response. These findings support LIC11574 and LIC13411 as promising sources of B-cell peptide epitopes for the development of multi-epitope vaccines against leptospirosis. Further studies should validate their immunogenicity in vivo, optimize delivery systems, and assess stability.</p>

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Bioinformatics-based B-cell epitope identification from Leptospira interrogans outer membrane proteins LIC11574 and LIC13411 for the rational development of a multi-epitope anti-Leptospira vaccine

  • 期刊论文

  • 发表日期：

    2026年5月30日

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  • Jason M. Porcalla,
  • Princes Angela P. Podiotan,
  • Sedrick Maru M. Gutierrez,
  • Nedrick T. Distor

摘要

Leptospirosis is a globally neglected zoonotic disease caused by the spirochete Leptospira interrogans, posing a major public health burden in tropical and subtropical regions. Although antibiotic therapy remains the primary treatment for most bacterial infections, L. interrogans has exhibited increasing resistance to antimicrobial agents, underscoring the need for alternative prophylactic strategies and prompting further research into B-cell peptide epitope-based vaccines as a long-term solution for disease control. This study explored the outer membrane proteins LIC11574 and LIC13411 as sources of B-cell epitopes for rational vaccine development. Using bioinformatics and immune simulations, candidate epitopes were identified based on antigenicity, non-allergenicity, and immunogenicity. A total of 69 16-mer and 68 18-mer epitopes were identified in LIC11574, while LIC13411 yielded 112 16-mer and 123 18-mer epitopes. Structural investigation revealed that the identified B-cell peptide epitopes were predominantly located within α-helical regions, whereas the remaining sequences were distributed across β-sheet structures and loop regions. The top-ranked B-cell peptide epitopes of LIC11574 and LIC13411, selected for their antigenic and non-allergenic characteristics, were successfully docked with the HLA-DRB1*15 molecule, exhibiting promising binding affinities ranging from − 12.6 to − 14.9 kcal/mol. Immune simulations also revealed that the constructed multi-epitope vaccines induced B-cell and helper T-cell activities, indicating a favorable host immune response. These findings support LIC11574 and LIC13411 as promising sources of B-cell peptide epitopes for the development of multi-epitope vaccines against leptospirosis. Further studies should validate their immunogenicity in vivo, optimize delivery systems, and assess stability.