ArticleIranian journal of microbiology2023
Improvement the expression and purification of Loa22: a lipoprotein with OmpA domain from pathogenic
Article in Iranian journal of microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 2 citations in OpenAlex.
- Expression and Immunogenicity Analysis of Recombinant Leptospira Interrogans Surface Protein LigA in Mouse Model.Veterinary medicine and science · 2025Article
- Design, Development and Immunogenic Evaluation of a Novel Lipl32 Recombinant Protein of Local Pathogenic Leptospira Serovars.Archives of Razi Institute · 2025Article
- Recombinant outer membrane protein Lipl41 fromIranian journal of microbiology · 2024Article
- Immunological characterization of recombinant outer membrane Loa22 protein of local pathogenicVeterinary research forum : an international quarterly journal · 2024Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background and Objectives: One of the highly conserved outer membrane proteins expressed only by pathogenic Leptospires is Loa22. The study aims is to achieve the optimum conditions for high expression of recombinant Loa22 (rLoa22) protein. Materials and Methods: Complete coding sequence of Results: SDS-PAGE analysis showed that high production of rLoa22 protein obtained when post induction incubation, IPTG concentration, and duration of induction were 37°C, 0.1 M and 5 h in 2×TY medium respectively. The purification of rLoa22 protein under native conditions using Ni-NTA pull-down was optimum in one hour binding at 37°C, five times washing process and elution buffer with a pH 7.4 and a 0.3 M imidazole concentration. Conclusion: The findings of the study led to high production of pure Loa22 protein, which can form the basis for future investigation on the design of rapid diagnostic tests and more effective vaccine candidates for leptospirosis.
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