Structure-based Computational analysis of Protein Binding sites for Function and Druggability in Macrophage Infectivity Potentiator (MIP) Protein of Legionella pneumophila

Order of Publishing in Issue: 
Volume :7
Issue :4
October, 2013
Page No: 
C. Kumaraswamy Naidu and Y. Suneetha
Department of Zoology, Sri Venkateswara University, Tirupati – 517502, India.

Legionaries Disease is one of the top 10 bacterial infections in the world occurring to humans. The bacterial infection of Legionaries Disease, survive in wet environments. The infection will cause symptoms similar to the flu, but if not taken care of early, can cause renal disease. The macrophage infectivity potentiator (MIP) protein is a major virulence factor of Legionella pneumophila, the causative agent of Legionnaires’ disease. MIP belongs to the FK506-binding proteins (FKBP) and is necessary for optimal intracellular survival and lung tissue dissemination of L. pneumophila. In the present study, we used Virtual screening approach to successfully find an inhibitor against L. pneumophila MIP. Results showed that (4-{(2R)- 2-[(1S,3S,5S)-3,5-dimethyl-2-oxocyclohexyl]-2- hydroxyethyl}-2,6-dioxopiperidin-1-yl)acetate can act as a novel inhibitor against L. pneumophila MIP.

Legionaries Disease; Legionella pneumophila; Macrophage infectivity potentiator protein; Molecular docking.
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