Title

Authors

Digvijay Singh Chauhan¹, Sharat Chandra¹, Arun Gupta² & Tiratha Raj Singh^{1, 3}

Affiliation

¹Bioinformatics Sub-Centre, School of Biotechnology, Devi Ahilya University, Indore-452001; ²School of Computer Science and Information Technology, Devi Ahilya University, Indore-452001; ³Dpartment of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Solan-173234, H.P, India.

Email

tiratharaj@gmail.com; *Corresponding author

Article Type

Hypothesis

Date

Received February 08, 2012; Accepted February 11, 2012; Published February 28, 2012

Salmonella enteric serovar Typhi Ty2 is a human specific pathogen and an etiological agent for typhoid fever. Most of Salmonella serotypes produce glycogen which has a comparatively minor role in virulence and colonization, but has a more significant role in survival. Enzymes present in glycolytic pathway of bacteria help bacteria to survive by activating other factors inside host. Numerous pathogenic bacteria species intervene with the plasminogen system, and this plasminogen–enolase association may play a critical role in the virulence of S. Typhi by causing direct damage to the host cell extracellular matrix, possibly by enzymic degradation of extracellular matrix proteins or other protein constituents. In this study, molecular modelling of enolase of Salmonella has been accomplished in silico by comparative modelling; we have then analyzed Human alpha enolase which is a homodimer and serves on epithelial cells with our model. Both Structures were docked by D-tartronate semialdehyde phosphate (TSP) and 3-aminoenolpyruvate phosphate (AEP) enolase inhibitors. Our study shows that salmonella enolase and human enolase have different active sites in their structure. This will help in development of new ligands, more suitable for inhibiting bacterial survival inside host as vaccines for typhoid fever are not fully protective. The study also confirmed that enolase Salmonella and Human Plasminogen suggested direct physical interaction between both of them as the activation loop of plasminogen residues showed conformational changes similar to the tissue type plasminogen activator. Various computational biology tools were used for our present study such as Modeller, Molegro Virtual Docker, Grommacs.

Keywords

Salmonella Ty2, Enolase, TSP (D-tartronate semialdehyde phosphate), AEP (3-aminoenolpyruvate phosphate), Modelling, Docking.

Citation

Chauhan et al. Bioinformation 8(4): 185-188 (2012)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.