Ceftobiprole

Ceftobiprole Uses, Dosage, Side Effects, Food Interaction and all others data.

Ceftobiprole is a cephalosporin antibiotic with activity against methicillin-resistant Staphylococcus aureus. It was discovered by Basilea Pharmaceutica and is being developed by Johnson & Johnson Pharmaceutical Research and Development. Ceftobiprole is the first cephalosporin to demonstrate clinical efficacy in patients with infections due to methicillin-resistant staphylococci and, if approved by regulatory authorities, is expected to be a useful addition to the armamentarium of agents for the treatment of complicated skin infections and pneumonia.

Ceftobiprole, a cephalosporin antibiotic, is active against methicillin-resistant Staphylococcus aureus.

Ceftobiprole
Uses
Dosage
Side Effect
Precautions
Interactions
Uses during Pregnancy
Uses during Breastfeeding
Accute Overdose
Food Interaction
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Interaction With other Medicine
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Trade Name	Ceftobiprole
Generic	Ceftobiprole
Ceftobiprole Other Names	Ceftobiprol, Ceftobiprole
Type
Formula	C₂₀H₂₂N₈O₆S₂
Weight	Average: 534.57 Monoisotopic: 534.110372808
Groups	Approved, Investigational
Therapeutic Class
Manufacturer
Available Country
Last Updated:	September 19, 2023 at 7:00 am

Uses

Ceftobiprole is a cephalosporin antibiotic used to treat both community and hospital-acquired pneumonia caused by susceptible bacteria.

For the treatment of serious bacterial infections in hospitalised patients.

Ceftobiprole is also used to associated treatment for these conditions: Community Acquired Pneumonia (CAP), Nosocomial Pneumonia

How Ceftobiprole works

Cephalosporins, such as ceftobiprole, are bactericidal and have the same mode of action as other beta-lactam antibiotics (such as penicillins). Cephalosporins disrupt the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity, especially in Gram-positive organisms. The final transpeptidation step in the synthesis of the peptidoglycan is facilitated by transpeptidases known as penicillin binding proteins (PBPs). PBPs bind to the D-Ala-D-Ala at the end of muropeptides (peptidoglycan precursors) to crosslink the peptidoglycan. Beta-lactam antibiotics mimic this site and competitively inhibit PBP crosslinking of peptidoglycan.