Evidence map›Paper›PMID 42217038›Full record

ArticleArchives of microbiology2026

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.

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

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Article in Archives of microbiology, 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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5 · Who and what money

Authors and funding

4 authors.

Jason M Porcalla *Department of Chemistry and Biochemistry, College of Allied Sciences, De La Salle Medical and Health Sciences Institute, Cavite, Philippines.
Princes Angela P Podiotan *Department of Chemistry and Biochemistry, College of Allied Sciences, De La Salle Medical and Health Sciences Institute, Cavite, Philippines.
Sedrick Maru M Gutierrez *Department of Chemistry and Biochemistry, College of Allied Sciences, De La Salle Medical and Health Sciences Institute, Cavite, Philippines.
Nedrick T DistorDepartment of Biology and Biochemistry, University of Houston, Houston, TX, USA. ntdistor@uh.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Bacterial Outer Membrane ProteinsBacterial VaccinesEpitopes, B-LymphocyteLeptospira interrogansLeptospirosisAnimalsAntigens, BacterialComputational BiologyHumansImmunoinformaticsProtein Subunit VaccinesVaccine DevelopmentAntigens, BacterialBacterial Outer Membrane ProteinsBacterial VaccinesEpitopes, B-LymphocyteProtein Subunit VaccinesbioinformaticsimmunityLeptospirosisL. interroganspeptide epitopevaccine

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.