These proteins are needed for bacterial cell wall synthesis and are the targets of β-lactam antibiotics. The new penicillin-binding protein has low affinity to β-lactam antibiotics and is thus resistant to the drugs, and the bacteria survive treatment. This type of resistance is the basis in MRSA (methicillin-resistant Staphylococcus aureus).

The mechanism by which inhibition of penicillin-binding proteins by β-lactam agents causes bacterial lysis and death has been investigated for decades. Normal cell growth and division require the coordinated participation of both peptidoglycan synthetic enzymes and those with autolytic activity (murein, or peptidoglycan hydrolases; autolysins).

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Penicillin‐binding proteins (PBPs), membrane‐associated macromolecules which play key roles in the cell wall synthesis process, have been exploited for over 70 years as the targets of the highly successful β‐lactam antibiotics.

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Multiple Low-Reactivity Class B Penicillin-Binding Proteins Are Required for Cephalosporin Resistance in Enterococci. Enterococcus faecalis and Enterococcus faecium are commensals of the gastrointestinal tract of most terrestrial organisms, including humans, and are major causes of health care-associated infections.

B) are enzymes.

Natl. Acad. Sci. U.S.A. 72:2999-3003(1975) [ PubMed ] [ Europe PMC ] [ Abstract ] Bacterial proteins that share the property of binding irreversibly to PENICILLINS and other ANTIBACTERIAL AGENTS derived from LACTAMS.
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Binds penicillin-binding proteins (transpeptidases) Blocks transpeptidase cross-linking of peptidoglycan in cell wall. Activates autolytic enzymes. Penicillin MoA (4) Beta-lactamase cleaves the beta-lactam ring of penicillin. Mutations in penicillin-binding proteins.

In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex and the class-A penicillin-binding proteins (aPBPs). For decades, it was thought that only class A penicillin-binding proteins (PBPs) and related enzymes effected peptidoglycan synthesis.
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De binder till active site på enzymet PBP (penicillin binding protein) och hindrar det då från att binda till peptidoglykankedjor i cellväggen och skapa cross-links

PBPs are the specific targets for β-lactam antibiotics and critically involved in the late stages of peptidoglycan synthesis.