Phylogenetic and in silico Proteomic Analysis of Fructose 1, 6 Biphosphate Aldolase-II in Community Acquired-Methicillin Resistant Staphylococcus aureus (CA-MRSA)

In 1990s, a new strain of methicillin resistant Staphylococcus aureus (MRSA) emerged in the community setting occurring among young healthy individuals with no exposure to the healthcare setting. The infections caused by these strains are called community-acquired MRSA (CA-MRSA). Skin and soft-tissue infections (SSTIs) are the most common type of CA-MRSA infection including furuncles, abscesses, folliculitis, impetigo, cellulitis, and more rarely, in cases of severe sepsis, necrotizing fascitis, and necrotizing pneumonia. Recently, fructose 1, 6 biphosphate aldolase-II (FBA) enzyme has been identified as potential drug target for CA-MRSA through metabolic pathways analysis. In the present work, phylogenetic analysis and computational proteomic analysis of FBA for CA-MRSA was carried out. The phylogenetic analysis results of FBA in CA-MRSA reveal that apart from various S. aureus strains, it is closely related to other pathogenic non-aureus staphylococcal species as well. In addition, FBA is evolutionarily conserved in other pathogenic species of Bacillus. Therefore, FBA might be exploited as potential therapeutic drug target for various aureus and non-aureus species of Staphylococci. The proteomic analysis of FBA reveals that this protein belongs to Aldolase class-II family, which is absolutely distinct from the mammals. The physico-chemical properties data suggest that the FBA protein is stable in nature.