PBP2aPenicillin Binding Protein 2a
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These parameters include in oculum size, salt concentration, pH, composition of medium, osmolarity and temperature.13 After screening by phenotypic methods in clinical laboratories, chances of uncertainty are still present due to conditional manifestation of PBP2a. The results have to be confirmed by a gold standard which is fast, precise, sensitive and also independent of growth conditions14.
Properties of a novel PBP2A protein homolog from Staphylococcus aureus strain LGA251 and its contribution to the [beta]-lactam-resistant phenotype.
Discrepancies between phenotypic detection of methicillin resistance by VITEK 2 and negative results of a PBP2a detection kit, as well as negative mecA and mecC test results, by commercial and in-house PCRs led to the detection of a mecB-encoded methicillin resistance.
ATCC: American Type of Culture Collection CI: Confidence Interval CLSI: Clinical and Laboratory Standards Institute EPI-Info: Epidemiological Information MRSA: Methicillin Resistance Staphylococcus aureus MSSA: Methicillin Susceptible Staphylococcus aureus AOR: Adjusted odds ratio PBP2a: Penicillin binding protein S.A: Staphylococcus aureus S.
mecA gene that is responsible for resistance to methyl-penicillins including methicillin is located on a mobile staphylococcal cassette chromosome mec (SCCmec) elements and encodes an altered Penicillin Binding Protein (PBP2a), with low affinity for all [beta]-lactam antibiotics even in the same SCCmec type.
Subsequently, a scanning electron microscopy (SEM) analysis was chosen to evaluate the antibacterial effect from MFM501 on the cell structure of a selected MRSA isolate since earlier study has shown that the pyrrolidone ring plays an important role for the strong binding affinity to the penicillin-binding-protein 2a (PBP2a) site which could prevent cell wall synthesis in Staphylococci species as exemplified in ceftobiprole, a commercially available fifth-generation cephalosporin antibiotic which has a pyrrolidone ring on its chemical structure [4, 5].
MRSA has the capacity of synthesizing a variant of PBP2 called PBP2A, keeping its physiological function, but with low affinity to beta-lactams (Ito, Okuma, Ma, Yuzawa, & Hiramatsu, 2003; McCulloch, 2006).
However, the breakthrough this discovery had brought was short-lived as the bacteria evolved yet again, forming a new protein PBP2a, encoded by the mecA gene which replaced PBP1.
But one of these enzymes, PBP2A, which is induced when MRSA is exposed to beta-lactam antibiotics, is not rendered inactive by the antibiotics.
In addition to extracellular DNA, a number of different proteins are associated with ica-independent formation and accumulation of biofilm, including FnBPA and FNBPB, Spa, SasG, and more recently, PBP2a (11-16).