scholarly journals Characterization of a Catalase-Negative Methicillin-Resistant Staphylococcus aureus Strain

2007 ◽  
Vol 45 (8) ◽  
pp. 2684-2685 ◽  
Author(s):  
B. M. Gruner ◽  
S.-R. Han ◽  
H.-G. Meyer ◽  
U. Wulf ◽  
S. Bhakdi ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Aureus Strain ◽  
Methicillin Resistant

scholarly journals Proteomics and Docking Study Targeting Penicillin-Binding Protein and Penicillin-Binding Protein2a of Methicillin-Resistant Staphylococcus aureus Strain SO-1977 Isolated from Sudan

2019 ◽  
Vol 15 ◽  
pp. 117693431986494 ◽  
Author(s):  
Sofia B Mohamed ◽  
Talal A Adlan ◽  
Nagla A Khalafalla ◽  
Nusiba I Abdalla ◽  
Zainab SA Ali ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Docking Study ◽  
Binding Energies ◽  
Aureus Strain ◽  
Resistant Bacteria ◽  
Single Nucleotide ◽  
Methicillin Resistant ◽  
Hydrogen Bond Interactions

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.

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