No abstract

Whole genome sequencing of methicillin-resistant Staphylococcus aureus (MRSA) strain isolated from Sudan has led to a great deal of information, which allows the identification and characterization of some pivotal proteins. The objective of this study was to investigate the penicillin-binding proteins, PBP and PBP2a, of SO-1977 strain to have insights about their physicochemical properties and to assess and describe the interaction of some phytochemicals against them in silico. PBP and PBP2a from MRSA’s Sudan strain were found to be of great resemblance with some other strains. G246E single-nucleotide polymorphism was reported and identified in the allosteric binding site positioned in the non-penicillin-binding domain. The docked compounds demonstrated good binding energies and hydrogen bond interactions with residue Ser404 which plays crucial roles in β-lactam activity. This finding would contribute significantly to designing effective β-lactam drugs, to combat and treat β-lactam–resistant bacteria in the future.

This study aims to describe the global detection and functional inference of hypothetical protein CA803_03125 from Staphylococcus aureus SO-1977. Computational methods were utilized to study this protein based on sequence similarity and presence of known protein domains. The BLASTp result revealed a significant similarity between the hypothetical protein (CA803_03125) and ADP-ribose hydrolase protein from four S. aureus strains (MW2, MRSA252, COL, and N315). Evolutionary tree diagram revealed a close relationship between the hypothetical protein and proteins of MW2 and COL strains. The physicochemical characterization revealed that all proteins were found to be stable, soluble, hydrophilic and acidic in their nature. The Macro domain was found to exist within all proteins. Moreover, the proteins were of pronounced similarity in terms of primary, secondary and tertiary organization. The protein CA803_03125 (SO-1977) is already known and well characterized as ADP-ribose hydrolase; therefore, we would recommend that its NCBI data has to be updated to be submitted under the name of ADP-ribose hydrolase.