Back to Search
Start Over
Staphylococcus aureus Penicillin-Binding Protein 2 Can Use Depsi-Lipid II Derived from Vancomycin-Resistant Strains for Cell Wall Synthesis
- Source :
- Chemistry (Weinheim an Der Bergstrasse, Germany)
- Publication Year :
- 2013
- Publisher :
- WILEY-VCH Verlag, 2013.
-
Abstract
- Vancomycin-resistant Staphylococcus aureus (S. aureus) (VRSA) uses depsipeptide-containing modified cell-wall precursors for the biosynthesis of peptidoglycan. Transglycosylase is responsible for the polymerization of the peptidoglycan, and the penicillin-binding protein 2 (PBP2) plays a major role in the polymerization among several transglycosylases of wild-type S. aureus. However, it is unclear whether VRSA processes the depsipeptide-containing peptidoglycan precursor by using PBP2. Here, we describe the total synthesis of depsi-lipid I, a cell-wall precursor of VRSA. By using this chemistry, we prepared a depsi-lipid II analogue as substrate for a cell-free transglycosylation system. The reconstituted system revealed that the PBP2 of S. aureus is able to process a depsi-lipid II intermediate as efficiently as its normal substrate. Moreover, the system was successfully used to demonstrate the difference in the mode of action of the two antibiotics moenomycin and vancomycin.
- Subjects :
- Methicillin-Resistant Staphylococcus aureus
Staphylococcus aureus
Penicillin binding proteins
enzymes
vancomycin
Oligosaccharides
Peptidoglycan
Muramoylpentapeptide Carboxypeptidase
medicine.disease_cause
Catalysis
antibiotics
Cell wall
lipids
chemistry.chemical_compound
Muramoylpentapeptide carboxypeptidase
Cell Wall
Depsipeptides
medicine
Penicillin-Binding Proteins
Lipid II
Organic Chemistry
General Chemistry
Full Papers
Methicillin-resistant Staphylococcus aureus
Anti-Bacterial Agents
chemistry
Biochemistry
peptides
Vancomycin
medicine.drug
Subjects
Details
- Language :
- English
- ISSN :
- 15213765 and 09476539
- Volume :
- 19
- Issue :
- 36
- Database :
- OpenAIRE
- Journal :
- Chemistry (Weinheim an Der Bergstrasse, Germany)
- Accession number :
- edsair.doi.dedup.....0b6dc1d7bf2eee5a435016cb3278acb0