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BMC Microbiol. 2016 Oct 12;16(1):239.

Enterococcus hirae LcpA (Psr), a new peptidoglycan-binding protein localized at the division site.

Author information

1
Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium.
2
University Grenoble Alpes, IBS, Grenoble, F-38044, France.
3
CNRS, IBS, Grenoble, F-38044, France.
4
CEA, IBS, Grenoble, F-38044, France.
5
Physiologie et génétique bactérienne, Centre d'Ingénierie des Protéines, Université de Liège, Institut de Chimie, Liège, B-4000, Belgium. bjoris@ulg.ac.be.

Abstract

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.

KEYWORDS:

Bacterial division; Cell wall; Enterococcus; LytR-CpsA-Psr; Peptidoglycan

PMID:
27729019
PMCID:
PMC5059904
DOI:
10.1186/s12866-016-0844-y
[Indexed for MEDLINE]
Free PMC Article

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