Penicillin Binding Protein
Penicillin binding protein refers to an enzyme that catalyzes the final peptidoglycan biosynthesis stages in the periplasm. This enzyme is important for the growth as well as the division of the cells of bacteria. For a long time, this protein has been known to be vital for rod-shaped morphology in the gram-negative bacteria such as Escherichia coli as well as Pseudomonas aeruginosa. Most bacteria are characterized by the production of several PBPs for the metabolism of peptidoglycan. As such, this protein is a vital component in divisome, catalyzing the cross-linking of peptidoglycan of the cell wall at the time of cell division. This protein belongs to the acyl-serine transferases family and traditionally, proteins in this family are separated into low-molecular weight and high-molecular-weight on the basis of their molecular weight as well as the sequence homology.
What is the role of penicillin binding protein?
The major role of this protein is to synthesize as well as to remodel the peptidoglycan of the cell wall. This is an important component of the cell wall of bacteria because it gives rigidity and shape to the cell of bacteria. This protein is found in every bacteria and it represents the major targets in the anti-biotherapy, more so for β-lactam antibiotics that are used the most. PBPs are the major players in the cell cycle of bacteria as well as the processes of drug resistance. Formation of a daughter cell and cell division in bacteria is a complex mechanism with details that are orchestrated by several proteins. PBPs play a significant role in the synthesis of the cell wall. PBPs inhibition has been known to cause irregularities in the structure of the cell wall. Such irregularities include lesions, elongation, lysis, loss of selective cell wall permeability and eventual death of the cell.
Why is this protein important?
PBPs are important because they bind to the β-lactam antibiotics since they are the same in their chemical structure to molecular pieces that peptidoglycan is made of. By binding to the penicillin, β-lactam amide bond ruptures forming a covalent bond and residue of catalytic serine at the active site of the PBPs. This reaction is irreversible and it inactivates enzymes. Increase in the incidences of beta-lactam microorganism that are resistant as well as the progress that has been made in genetics, immunofluorescence microscopy and genomics have led to intensive study of this protein. This study has covered various bacterial species. Additionally, the publication of the high-resolution structures in PBPs from the pathogenic organisms has shed more light on the intertwining of drug resistance as well as the processes of cell division. All these issues have made this protein very important in the medical field.
How is penicillin binding protein used?
A lot of research has been done on PBPs because they play a significant role in resistance and antibiotics. The synthesis of the cell wall of bacteria and the role that PBPs play in the synthesis of this wall is a great target for various drugs with selective toxicity. This is because enzymes and metabolic pathways are unique to different bacteria. Antibiotics resistance has been caused by the overproduction of this protein as well as PBPs formation whose penicillin’s affinity is low including other mechanisms like lactamase production. PBPs’ research has made discovering new semi-synthetic β-lactams possible. These have made altering side-chains on original penicillin molecule increase PBPs affinity for penicillin. Thus, this has increased the effectiveness of bacteria when it comes to the development of resistance. The presence of PBP2A is what causes the antibiotic resistance that is seen in methicilin-resistant staphylococcus aureus.
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