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.
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