Please use this identifier to cite or link to this item: https://dspace.iiti.ac.in/handle/123456789/15149
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dc.contributor.authorSingh, Brijeshwaren_US
dc.contributor.authorKodgire, Prashanten_US
dc.date.accessioned2024-12-24T05:20:07Z-
dc.date.available2024-12-24T05:20:07Z-
dc.date.issued2024-
dc.identifier.citationSingh, B., & Kodgire, P. (2024). Refolding dynamics and immunoinformatic insights into Vibrio cholerae OmpA, OmpK, and OmpV for vaccine applications. International Journal of Biological Macromolecules. Scopus. https://doi.org/10.1016/j.ijbiomac.2024.137643en_US
dc.identifier.issn0141-8130-
dc.identifier.otherEID(2-s2.0-85209248506)-
dc.identifier.urihttps://doi.org/10.1016/j.ijbiomac.2024.137643-
dc.identifier.urihttps://dspace.iiti.ac.in/handle/123456789/15149-
dc.description.abstractOmpA, OmpK, and OmpV are crucial for the pathogenesis of Vibrio cholerae, functioning within the bacterium's outer membraneen_US
dc.description.abstractthey present significant potential as candidates for vaccine development. Due to their intrinsic β-sheet richness, these OMPs tend to form inclusion bodies whenever overexpression is attempted. To achieve a native-like structure, detergents can be utilized during the refolding of OMPs from inclusion bodies. The impact of different detergents is examined on the renaturation of these OMPs, specifically non-ionic and zwitterionic detergents. The findings provide valuable insights into detergent selection, with LDAO and DDM emerging as the best protein refolding agents, facilitating successful structural and functional studies of these OMPs. Furthermore, using immunoinformatics it is established that OmpA, OmpK, and OmpV carry B- and T-cell epitopes in their exposed extracellular regions. The presence of immunodominant regions makes it easier to employ these proteins as vaccine candidates as they are stable, non-allergenic, and likely to stimulate successful innate and active immune responses. Overall, with all three OMPs harboring numerous immunogenic epitopes, they can be employed in subunit vaccines against Vibrio spp. and contribute to the development of diagnostic tools for effective disease mitigation. © 2024 Elsevier B.V.en_US
dc.language.isoenen_US
dc.publisherElsevier B.V.en_US
dc.sourceInternational Journal of Biological Macromoleculesen_US
dc.subjectDetergentsen_US
dc.subjectImmunoinformaticsen_US
dc.subjectOuter membrane proteinsen_US
dc.subjectProtein refoldingen_US
dc.subjectVibrioen_US
dc.titleRefolding dynamics and immunoinformatic insights into Vibrio cholerae OmpA, OmpK, and OmpV for vaccine applicationsen_US
dc.typeJournal Articleen_US
Appears in Collections:Department of Biosciences and Biomedical Engineering

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