Abstract: The objective of this research was focused on investigating in vitro antimicrobial activity of Phellinus linteus fruiting body extracts on Pseudomonas aeruginosa, Escherichia coli, Staphylococcus aureus and Methicillin-resistant Staphylococcus aureus. Phellinus linteus fruiting body was extracted with ethanol and ethyl acetate and was vaporized. The disc diffusion assay was used to assess antimicrobial activity against tested bacterial strains. Primary screening of chemical profile of crude extract was determined by using thin layer chromatography. The positive control and the negative control were used as erythromycin and dimethyl sulfoxide, respectively. Initial screening of Phellinus linteus crude extract with the disc diffusion assay demonstrated that only ethanol had greater antimicrobial activity against Pseudomonas aeruginosa, Escherichia coli, Staphylococcus aureus and Methicillin-resistant Staphylococcus aureus. The MIC assay showed that the lower MIC was observed with 0.5 mg/ml of Pseudomonas aeruginosa and Methicillin-resistant Staphylococcus aureus and 0.25 mg/ml. of Escherichia coli and Staphylococcus aureus, respectively. TLC chemical profile of extract was represented at Rf ≈ 0.71-0.76.
Abstract: Methicillin/multiple-resistant Staphylococcus aureus
(MRSA) are infectious bacteria that are resistant to common
antibiotics. A previous in silico study in our group has identified a
hypothetical protein SAV1226 as one of the potential drug targets. In
this study, we reported the bioinformatics characterization, as well as
cloning, expression, purification and kinetic assays of hypothetical
protein SAV1226 from methicillin/vancomycin-resistant
Staphylococcus aureus Mu50 strain. MALDI-TOF/MS analysis
revealed a low degree of structural similarity with known proteins.
Kinetic assays demonstrated that hypothetical protein SAV1226 is
neither a domain of an ATP dependent dihydroxyacetone kinase nor
of a phosphotransferase system (PTS) dihydroxyacetone kinase,
suggesting that the function of hypothetical protein SAV1226 might
be misannotated on public databases such as UniProt and
InterProScan 5.