The expressions of PBPs in MRSA have been well documented in previous studies, with PBP-2 and PBP-3 proposed as the lethal targets for β-lactams action. The PBPs are inhibited by β-Lactam antibiotics such as methicillin and vancomycin by interrupting the biochemical functions at the D-Ala-D-Ala terminus of the peptidoglycan precursor. Penicillin-binding proteins (PBPs) are enzymes commonly expressed by MRSA during peptidoglycan synthesis, cell growth, and morphogenesis. The history of ever-increasing resistance among MRSA strains suggests that they are likely to be more prevalent in the future, thus severely restricting treatment options. Even though methicillin-resistant staphylococci produce penicillinase, blocking of this enzyme do not affect the level of methicillin resistance. The resistance of methicillin by Staphylococcus aureus has been documented to depend on several factors such as temperature, pH, NaCl concentration, and inoculum size. aureus (MRSA), at times with little success. Glycopeptides such as vancomycin and teicoplanin are often the choice in treating infections associated with methicillin-resistant S. Methicillin resistance (MR) by Staphylococcus aureus is a persistent clinical problem affecting many geographic locations worldwide. This report highlights structural features of PBP-2′ that can serve as targets for developing new chemotherapeutic agents and conducting site direct mutagenesis experiments. PBP-2′ has three striking regulatory points constituted by first penicillin binding site at Ser25, second penicillin binding site at Ser405, and finally a single metallic ligand binding site at Glu657 which binds to ions. Our analysis revealed that the PBP-2′ is very stable with more hydrophilic amino acids expressing antigenic sites. We conducted a complete structural and functional regulatory analysis of PBP-2′ protein. Presently, there is no structural and regulatory information on PBP-2′ protein. The PBP-2′ functions by substituting other penicillin binding proteins which have been inhibited by β-lactam antibiotics. A mechanism for resistance has been proposed in which methicillin resistant Staphylococcus aureus (MRSA) isolates acquired a new protein called β-lactam inducible penicillin binding protein (PBP-2′). Resistance to methicillin by Staphylococcus aureus is a persistent clinical problem worldwide.
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