Free Essay: Penicillin Binding Protein and how it Works in the Body
Defining penicillin binding proteins
Penicillin binding proteins are a group of proteins found in different organisms that have high affinity for penicillin and bind themselves to penicillin. These proteins are made up of many types of bacteria. They bind themselves in different ways and as such there are both cytoplasmic bound penicillin binding proteins and membrane bound ones.
Penicillin binding proteins are also different in size and scientists state that up to six different types of these proteins can be found in one bacterium strain. These proteins may range anywhere between 40000 to 91000 in molecular weight. Additionally, these proteins in occur in varying numbers for every cell and each protein has a different affinity for penicillin. There are also two different categories of the penicillin binding proteins and these include the high molecular weight and low molecular weight penicillin binding proteins.
The roles of penicillin binding protein
Despite their differences, each penicillin binding protein helps in synthesizing peptidoglycan. Basically peptidoglycan is a major component of bacterial cell walls and the penicillin binding proteins are involved in the final stages of its synthesis. The essence of this is that bacterial walls when synthesized promote growth of cells as well as cell division which eventually leads to reproduction. Synthesis of these bacterial walls also helps in maintenance of the cellular structure in bacteria.
This makes penicillin binding proteins very important in the reproduction and growth of every organism. When these penicillin binding proteins are inhibited, the cell wall experiences irregularities such as elongation, loss of selective permeability, redundant growth, lesions and eventual death. This can interfere with the functioning of the body.
In addition to this, penicillin binding proteins are used in catalyzing several reactions which are triggered by synthesis of peptidoglycan. These include catalyzing synthesis of cross linked peptidoglycan from lipid intermediates. The proteins also catalyze the removal of D-alanine from the peptidoglycan’s precursor.
There has been much debate about the link between penicillin binding proteins and their role in antibiotic and drug resistance in the body. Several researches have been carried out to determine how penicillin binding proteins may become ineffective leading to antibiotic resistance in the body.
When a patient is treated with small doses of penicillin, the drug attacks the bacteria and changes its shapes causing it to elongate and lose turgidity. As the dosage increases, the bacterial cells completely lose integrity and eventually burst. This helps in killing bacteria and fending off the bacterial diseases.
However, there have been cases where penicillin binding proteins have failed to execute their role in binding certain antibiotics effectively. Basically there are three main ways through which the body of the patient may develop resistance. There are cases where the bacteria change the penicillin binding proteins so that even when they perform their functions, they do not bind themselves to the drugs and hence cannot catalyze the reaction necessary to fight off the bacteria.
Another method in which the body may develop resistance is where bacteria develop effective ways of shielding sensitive enzymes from the antibiotics administered. This method may include the bacteria pumping the penicillin bound drugs away from the cell hence evading destruction.
The last and most effective method of penicillin resistance developed by the bacteria is creation of a special enzyme which is called pecillinase or beta-lactamase. This enzyme seeks out the drugs administered and destroys them.
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