Abstract
Methicillin-resistant Staphylococcus aureus (MRSA) infection is a global health concern that has caused severe health threats over the past decade. Leaves extract of C. odontophyllum has been proven previously as an anti MRSA agent. Proteomics provide a technique that used to analyze the differential of protein expression profile between untreated and treated MRSA with subinhibitory concentrations of acetone extract from C. odontophyllum leaves. This study aims to determine the optimum parameter for analysis of protein expression profile using two-dimension gels electrophoresis (2-DE) for MRSA protein after treatment with acetone extract from C. odontophyllum leaves. Comparison of the Protein Expression Profile (PEP) between the untreated and treated MRSA was analyzed using PDQuest software. The optimum condition for MRSA protein treated with acetone extract from C. odontophyllum leaves to produce the best resolution with greater spot distribution was as follows: 100 μg volume of MRSA protein that loaded after passive rehydration then was run until reaching 25 kVrhs during IEF using 17 cm IPG strip within ranges of pH 4 - 7. Analysis of protein expression from the 2-DE gel map shows that 9 protein spots up-regulated and 41 protein spots were down-regulated with more than 2-fold differences (p C. odontophyllum leave may provide an insight into the antimicrobial mechanism, which could lead to the identification of target protein for future novel therapeutic development against MRSA infections.
Highlights
Infectious diseases have been a leading cause of death worldwide
This study aims to determine the optimum parameter for analysis of protein expression profile using two-dimension gels electrophoresis (2-DE) for Methicillin-resistant Staphylococcus aureus (MRSA) protein after treatment with acetone extract from C. odontophyllum leaves
The optimum condition for MRSA protein treated with acetone extract from C. odontophyllum leaves to produce the best resolution with greater spot distribution was as follows: 100 μg volume of MRSA protein that loaded after passive rehydration was run until reaching 25 kVrhs during isoelectric focusing (IEF) using 17 cm IPG strip within ranges of pH 4 - 7
Summary
Infectious diseases have been a leading cause of death worldwide. The rapid emergence and spread of drug-resistant organisms such as MRSA have posed a significant public health burden. MRSA is strain of S. aureus with the presence of the mecA gene that encodes PBP2a, which is a cause of resistance in all β-lactam antibiotics [2]. The MRSA strains have been reported resistant against penicillins, cephalosporins, combinations of monobactams and carpenems and combinations of beta-lactam/beta-lactamase inhibitor [5]. HA-MRSA infection was acquired from the healthcare center while CA-MRSA infections acquired through the community Both HA-MRSA and CA-MRSA were significant factors of severe infections such as endocarditis, pneumonia, toxic shock syndrome, osteomyelitis and bacteraemia with a high rate of morbidity and mortality [5]. The MRSA infection causes a public health and economic burden worldwide through the longer length of stay and higher in-hospital mortality rate, antibiotic medication costs and total hospitalization costs [8]
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