STRUCTURAL CHARACTERIZATION OF LEGIONELLOSIS DRUG TARGET CANDIDATE ENZYME PHOSPHOMANNOMUTASE FROM LEGIONELLA PNEUMOPHILA STRAIN PARIS: AN IN SILICO APPROACH

Abstract

The harshness of legionellosis differs from mild Pontiac fever to potentially fatal Legionnaire’s disease. The increasingdevelopment of drug resistance against legionellosis has led to explore new novel drug targets. It has been found thatphosphoglucosamine mutase, phosphomannomutase, and phosphoglyceromutase enzymes can be used as the mostprobable therapeutic drug targets through extensive data mining. Phosphomannomutase isconcerned in a process called glycosylation.The purpose of this study was to predict the potential target of that specific drug. For this,the 3D structure of Phosphomannomutase of Legionella pneumophila (strain Paris) was determined by means ofhomology modeling through Phyre2 and refined by ModRefiner. The designed model was evaluated with a structurevalidation program, for instance, PROCHECK, Verify3D, and QMEAN, for further structural analysis. Secondary structural features were determined through self-optimized prediction method with alignment (SOPMA) and interacting networks by STRING. The analytical result of PROCHECK showedthat 91.0% of the residues are in the most favored region, 8.50% are in the additional allowed region of the Ramachandran plot. Verify3D graph value indicates a score of 0.77 and 0.91 for QMEAN respectively. The findings of this current study along with further extensive investigation may assist drug design against Legionellosis.