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Comparison of Leptospira interrogans and Leptospira biflexa genomes: analysis of potential leptospiral-host interactions

Mehrotra, Prachi and Ramakrishnan, Gayatri and Dhandapani, Gunasekaran and Srinivasan, Narayanaswamy and Madanan, Madathiparambil G (2017) Comparison of Leptospira interrogans and Leptospira biflexa genomes: analysis of potential leptospiral-host interactions. In: MOLECULAR BIOSYSTEMS, 13 (5). pp. 883-891.

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Official URL: http://dx.doi.org/10.1039/c6mb00856a

Abstract

Leptospirosis, a potentially life-threatening disease, remains the most widespread zoonosis caused by pathogenic species of Leptospira. The pathogenic spirochaete, Leptospira interrogans, is characterized by its ability to permeate human host tissues rapidly and colonize multiple organs in the host. In spite of the efforts taken to comprehend the pathophysiology of the pathogen and the heterogeneity posed by L. interrogans, the current knowledge on the mechanism of pathogenesis is modest. In an attempt to contribute towards the same, we demonstrate the use of an established structure-based protocol coupled with information on subcellular localization of proteins and their tissue-specificity, in recognizing a set of 49 biologically feasible interactions potentially mediated by proteins of L. interrogans in humans. We have also presented means to adjudge the physicochemical viability of the predicted host-pathogen interactions, for selected cases, in terms of interaction energies and geometric shape complementarity of the interacting proteins. Comparative analyses of proteins of L. interrogans and the saprophytic spirochaete, Leptospira biflexa, and their predicted involvement in interactions with human hosts, aided in underpinning the functional relevance of leptospiral-host protein-protein interactions specific to L. interrogans as well as those specific to L. biflexa. Our study presents characteristics of the pathogenic L. interrogans that are predicted to facilitate its ability to persist in human hosts.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the ROYAL SOC CHEMISTRY, THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Depositing User: Id for Latest eprints
Date Deposited: 03 Jun 2017 09:38
Last Modified: 03 Jun 2017 09:38
URI: http://eprints.iisc.ac.in/id/eprint/57098

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