Leptospiral imelysin (LIC_10713) is secretory, immunogenic and binds to laminin, fibronectin, and collagen IV

Sarma, Abhijit; Dhandapani, Gunasekaran; Phukan, Homen; Baby, A. Ebenezer; Hariharan, S.; De, Arun Kumar; Bhattacharya, Debasis; Natesan, Sankar; Tennyson, Jebasingh; Madanan, Madathiparambil G.

doi:10.1007/s00253-023-12573-6

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“…Leptospira OMPs were extracted following the Triton X-114 fractionation protocol with slight modifications. ,− Briefly, the harvested Leptospira cells pellet was subjected to Triton X-114 extraction buffer containing 10 mM Tris-cl (pH 8), 1% Triton X-114, and 150 mM NaCl at the rate of 1 mL per Leptospira pellet harvested from 25 mL culture followed by overnight incubation at 4 °C. The extract was centrifuged at 15000 g for 30 min at 4 °C.…”

Section: Methodsmentioning

confidence: 99%

Physiological Temperature and Osmotic Changes Drive Dynamic Proteome Alterations in the Leptospiral Outer Membrane and Enhance Protein Export Systems

Phukan,

Sarma,

Rex

et al. 2023

J. Proteome Res.

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Leptospirosis, a remerging zoonosis, has no effective vaccine or an unambiguous early diagnostic reagent. Proteins differentially expressed (DE) under pathogenic conditions will be useful candidates for antileptospiral measures. We employed a multipronged approach comprising high-resolution TMT-labeled LC-MS/MS-based proteome analysis coupled with bioinformatics on leptospiral proteins following Triton X-114 subcellular fractionation of leptospires treated under physiological temperature and osmolarity that mimic infection. Although there were significant changes in the DE proteins at the level of the entire cell, there were notable changes in proteins at the subcellular level, particularly on the outer membrane (OM), that show the significance of subcellular proteome analysis. The detergent-enriched proteins, representing outer membrane proteins (OMPs), exhibited a dynamic nature and upregulation under various physiological conditions. It was found that pathogenic proteins showed a higher proportion of upregulation compared to the nonpathogenic proteins in the OM. Further analysis identified 17 virulent proteins exclusively upregulated in the outer membrane during infection that could be useful for vaccine and diagnostic targets. The DE proteins may aid in metabolic adaptation and are enriched in pathways related to signal transduction and antibiotic biosynthesis. Many upregulated proteins belong to protein export systems such as SEC translocase, T2SSs, and T1SSs, indicating their sequential participation in protein transport to the outer leaflet of the OM. Further studies on OM-localized proteins may shed light on the pathogenesis of leptospirosis and serve as the basis for effective countermeasures.

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