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Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site
Maxime Maréchal1, Ana Amoroso1, Cécile Morlot2,3,4
1Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium.
Insights
The LytR-CpsA-Psr family protein LcpA in Enterococcus hirae is crucial for cell wall metabolism. This study characterizes LcpA, revealing its role in peptidoglycan binding and localization at the cell division site.
Area of Science:
- Microbiology
- Bacterial Cell Wall Biology
- Protein Function Characterization
Background:
- LytR-CpsA-Psr family proteins are widespread in Gram-positive bacteria.
- Functions of LytR-CpsA-Psr family proteins (LCPs) in enterococci are largely uncharacterized.
- The Psr protein from Enterococcus hirae, renamed LcpA, was previously linked to PBP5 expression and beta-lactam resistance.
Purpose of the Study:
- To characterize the LcpA protein from Enterococcus hirae.
- To investigate the function and localization of LcpA within the bacterial cell.
Main Methods:
- Protein production and purification (with and without transmembrane helix).
- Subcellular localization studies using various methods and in silico predictions.
- Interaction assays with Enterococcus hirae cell wall and peptidoglycan.
- Immunolocalization experiments.
Main Results:
- LcpA protein was successfully produced and purified.
- LcpA is localized in the membrane and binds to enterococcal peptidoglycan.
- LcpA and PBP5 were found to co-localize at the cell division site.
Conclusions:
- LcpA belongs to the LytR-CpsA-Psr family and plays a role in cell wall metabolism.
- LcpA likely functions as a phosphotransferase, attaching cell wall polymers to peptidoglycan.
- Findings support LcpA's involvement in maintaining cell wall integrity in enterococci.
Background:
Proteins from the LytR-CpsA-Psr family are found in almost all Gram-positive bacteria. Although LCP proteins have been studied in other pathogens, their functions in enterococci remain uncharacterized. The Psr protein from Enterococcus hirae, here renamed LcpA, previously associated with the regulation of the expression of the low-affinity PBP5 and β-lactam resistance, has been characterized.
Results:
LcpA protein of E. hirae ATCC 9790 has been produced and purified with and without its transmembrane helix. LcpA appears, through different methods, to be localized in the membrane, in agreement with in silico predictions. The interaction of LcpA with E. hirae cell wall indicates that LcpA binds enterococcal peptidoglycan, regardless of the presence of secondary cell wall polymers. Immunolocalization experiments showed that LcpA and PBP5 are localized at the division site of E. hirae.
Conclusions:
LcpA belongs to the LytR-CpsA-Psr family. Its topology, localization and binding to peptidoglycan support, together with previous observations on defective mutants, that LcpA plays a role related to the cell wall metabolism, probably acting as a phosphotransferase catalyzing the attachment of cell wall polymers to the peptidoglycan.
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