Next Article in Journal / Special Issue
Recent Advances in Multi-Drug Resistance (MDR) Efflux Pump Inhibitors of Gram-Positive Bacteria S. aureus
Previous Article in Journal
Efficacy and Safety of Procalcitonin-Guided Antibiotic Therapy in Lower Respiratory Tract Infections
Previous Article in Special Issue
Multidrug Efflux Systems in Helicobacter cinaedi
Article Menu

Export Article

Open AccessArticle
Antibiotics 2013, 2(1), 11-27; doi:10.3390/antibiotics2010011

The Staphylococcus aureus Membrane Protein SA2056 Interacts with Peptidoglycan Synthesis Enzymes

Institute of Medical Microbiology, University of Zurich / Gloriastrasse 32, 8006 Zurich, Switzerland
Centre of Quality Control in Microbiology / ul. Chelmska 30/34, 00-725 Warsaw, Poland
AMSolutions, ul. Debowa 32, 05-123 Chotomow, Poland
Institute for Medical Microbiology, Immunology and Parasitology, University of Bonn / Meckenheimer Allee 168, 53115 Bonn, Germany
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa / Av. Da Républica (EAN), 2781-901 Oeiras, Portugal
Author to whom correspondence should be addressed.
Received: 24 December 2012 / Revised: 16 January 2013 / Accepted: 16 January 2013 / Published: 22 January 2013
View Full-Text   |   Download PDF [669 KB, uploaded 25 January 2013]   |  


The yet uncharacterized membrane protein SA2056 belongs to the ubiquitous RND (Resistance-Nodulation-cell Division) family of transmembrane efflux transporters. The sa2056 gene is located downstream of femX, the gene encoding the essential, non-ribosomal peptidyl-transferase adding the first glycine in the staphylococcal cell wall pentaglycine interpeptide. Due to its proximity to and weak co-transcription with femX, we assumed that sa2056 may somehow be involved in peptidoglycan synthesis. Specific antibodies against SA2056 showed that this protein is expressed during growth and present in the membrane fraction of cell preparations. Using a bacterial two hybrid system, SA2056 was shown to interact (i) with itself, (ii) with FemB, which adds glycines 4 and 5 to the peptidoglycan interpeptide and (iii) with the essential penicillin binding proteins, PBP1 and PBP2, required for cell division and incorporation of the peptidoglycan into the cell wall. Unexpectedly, deletion of sa2056 led to no phenotype regarding growth, antibiotic resistances or cell morphology; nor did sa2056 deletion in combination with femB inactivation alter b-lactam and lysostaphin sensitivity and resistance, respectively, pointing to possible redundancy in the cell wall synthesis pathway. These results suggest an accessory role of SA2056 in S. aureus peptidoglycan synthesis, broadening the range of biological functions of RND proteins. View Full-Text
Keywords: Staphylococcus aureus; RND protein; FemABX; PBP; peptidoglycan; bacterial two-hybrid system Staphylococcus aureus; RND protein; FemABX; PBP; peptidoglycan; bacterial two-hybrid system

Figure 1

This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Quiblier, C.; Luczak-Kadlubowska, A.; Holdener, E.; Alborn, D.; Schneider, T.; Wiedemann, I.; Pinho, M.G.; Sahl, H.-G.; Rohrer, S.; Berger-Bächi, B.; Senn, M.M. The Staphylococcus aureus Membrane Protein SA2056 Interacts with Peptidoglycan Synthesis Enzymes. Antibiotics 2013, 2, 11-27.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Antibiotics EISSN 2079-6382 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top