In-silico investigation of virulence factors associated with Pseudomonas aeruginosa

Development of multi-drug resistance (MDR) in P. aeruginosa has made its treatment difficult. There is crucial need of novel compounds that could serve as alternatives to antibiotics. Designing of new drugs require understanding of the proteins associated with virulence of this pathogen. In current study, three virulence factors. i. e., exotoxin A (ETA), elastases (lasB) and serralysin (AprA) were analyzed. Amino acid sequences of these factors were retrieved from UNIPROT database and analyzed for physicochemical attributes, secondary and tertiary configurations via PROTPARAM and SOPMA tools and ALPHAFOLD protein database. All factors exhibited instability index, aliphatic index and extinction coefficients in the range of 19.21 to 38.80, 73.49 to 88.78 and 64750 to 92820, respectively, with negative values for GRAVY (-0.223 to -0.271). The 2D structural analysis revealed alpha helix, extended strand and random coil contents of these factors ranging between 14.82 to 34.53 %, 95 to 118 % and 52.51 to 963.47 %, respectively. Three structural domains with highly complex folding was observed in 3D configuration of ETA. The characteristics explored in current study might be used for designing the inhibitors of these virulence factors in future.