ArticleVeterinary medicine and science2025
Expression and Immunogenicity Analysis of Recombinant Leptospira Interrogans Surface Protein LigA in Mouse Model.
Article in Veterinary medicine and science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
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Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
backgroundPathogenic strains of spirochetes of Leptospira spp. cause a globally distributed zoonotic disease called leptospirosis. The disease has several clinical manifestations, ranging from asymptomatic and subclinical infection to fatal and severe forms. HYPOTHESIS/
objectivesThe aim of this study was to produce a recombinant Leptospiral immunoglobulin-like surface protein-A (r-LigA) antigen of Leptospira interrogans in a prokaryotic expression system and to assess its efficacy in a mouse model. MATERIALS AND
methodsThe optimal epitopes of the LigA protein were identified via bioinformatics studies. The pET32a
resultsBioinformatics analysis identified the key antigenic region of LigA spanning amino acids 852 to 1210. Colony PCR and digestion confirmed the successful transformation. Induction using 0.5 mM IPTG at 30°C for 5 h was found to be optimal. Overexpression of r-LigA under optimised conditions accumulated proteins as inclusion bodies. Purification of r-LigA under native conditions using optimised Ni-NTA yielded 1050 µg/mL protein and high immunogenicity by effectively stimulating the immune system in female Balb/C mice.
conclusionsThese findings support r-LigA as a strong candidate for future leptospirosis diagnostic tools and subunit vaccine development.
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