The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Recruitment of penicillin‐binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
Open accessAbstract
Summary: Staphylococcus aureus penicillin‐binding protein PBP2 is an enzyme involved in the last stages of peptidoglycan assembly and is an important player in the mechanism of methicillin resistance of this pathogen. PBP2 localized to the division site but its recruitment to the forming division septum was prevented after acylation by oxacillin. The presence of the antibiotic did not affect FtsZ ring maintenance nor the localization of externalized peptidoglycan precursors. Delocalization of PBP2 was also observed when its pentapeptide substrate was eliminated by addition of d‐cycloserine or blocked by addition of vancomycin. Taken together these observations suggest that PBP2 is recruited to the division site by binding to its substrate, which is localized at that place. In methicillin‐resistant S. aureus, addition of oxacillin does not result in delocalization of PBP2 indicating that acylated PBP2 can be maintained in place by functional PBP2A, the central element of this resistance mechanism.
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Cites
Structure, biochemistry and mechanism of action of glycopeptide antibiotics
Reynolds, P. E. (1989) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/bf01967563 · Cited by 699
Cited by
The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis
Sauvage, E., Kerff, F., Terrak, M., Ayala, J. A., & Charlier, P. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2008.00105.x · Cited by 1,317
Howden, B. P., Davies, J. K., Johnson, P. D. R., Stinear, T. P., & Grayson, M. L. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00042-09 · Cited by 962
FtsZ and the division of prokaryotic cells and organelles
Margolin, W. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1745 · Cited by 631
Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli
Vollmer, W., & Bertsche, U. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.06.007 · Cited by 451
Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes
Macheboeuf, P., Contreras-Martel, C., Job, V., Dideberg, O., & Dessen, A. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00024.x · Cited by 447
Metadata
- Authors
- Pinho, M. G., & Errington, J.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2004-11-25
- Volume
- 55
- Issue
- 3
- Pages
- 799-807
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2115278168
- Cited by
- 168
- References
- 1
- FWCI
- 5.93
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Pinho, M. G., & Errington, J. (2005). Recruitment of penicillin‐binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.2004.04420.x
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
