Penicillin-binding proteins: Difference between revisions

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== Penicillin-binding proteins ==
<gallery>
File:3OC2_Wiki.png|Structure of a penicillin-binding protein
File:Penicillin_inhibition.svg|Mechanism of penicillin inhibition
File:Penicillin_Binding_Protein_3_and_Carbenicillin_Interaction.png|Interaction of penicillin-binding protein 3 with carbenicillin
File:Penicillin_Core.svg|Core structure of penicillin
File:Filamentation_1.jpg|Penicillin-binding proteins
</gallery>

Latest revision as of 04:39, 18 February 2025

Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity to and binding of penicillin. They are a crucial component of the bacterial cell wall synthesis.

Function[edit]

PBPs are involved in the final stages of constructing the bacterial cell wall, which is essential for the bacteria's survival. They catalyze a number of processes including the cross-linking of the peptidoglycan polymers that give the cell wall its strength.

Interaction with Penicillin[edit]

Penicillin and other beta-lactam antibiotics inhibit PBPs, which disrupts cell wall synthesis and leads to cell death. This is the primary mode of action of these antibiotics.

Types of PBPs[edit]

There are several types of PBPs, each with a specific role in cell wall synthesis. These include:

  • High molecular weight PBPs: These are involved in the cross-linking of the peptidoglycan polymers.
  • Low molecular weight PBPs: These are involved in other aspects of cell wall synthesis, such as the modification of the peptidoglycan polymers.

Resistance to Penicillin[edit]

Some bacteria have developed resistance to penicillin and other beta-lactam antibiotics. This is often due to the production of beta-lactamase enzymes, which break down the antibiotic and render it ineffective. However, some bacteria have also developed altered PBPs that have a lower affinity for penicillin, reducing the antibiotic's effectiveness.

See Also[edit]

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PubMed
Wikipedia

Penicillin-binding proteins[edit]