In:
Molecular Microbiology, Wiley, Vol. 99, No. 3 ( 2016-02), p. 546-556
Abstract:
Bacteria remodel peptidoglycan structure in response to environmental changes. Many enzymes are involved in peptidoglycan metabolism; however, little is known about their responsiveness in a defined environment or the modes they assist bacteria to adapt to new niches. Here, we focused in peptidoglycan enzymes that intracellular bacterial pathogens use inside eukaryotic cells. We identified a peptidoglycan enzyme induced by S almonella enterica serovar Typhimurium in fibroblasts and epithelial cells. This enzyme, which shows γ‐D‐glutamyl‐ meso ‐diaminopimelic acid D , L ‐endopeptidase activity, is also produced by the pathogen in media with limited nutrients and in resting conditions. The enzyme, termed EcgA for e ndopeptidase responding to c essation of g rowth’, is encoded in a S . Typhimurium genomic island absent in E scherichia coli . EcgA production is strictly dependent on the virulence regulator PhoP in extra‐ and intracellular environments. Consistent to this regulation, a mutant lacking EcgA is attenuated in the mouse typhoid model. These findings suggest that specialised peptidoglycan enzymes, such as EcgA , might facilitate S almonella adaptation to the intracellular lifestyle. Moreover, they indicate that readjustment of peptidoglycan metabolism inside the eukaryotic cell is essential for host colonisation.
Type of Medium:
Online Resource
ISSN:
0950-382X
,
1365-2958
DOI:
10.1111/mmi.2016.99.issue-3
Language:
English
Publisher:
Wiley
Publication Date:
2016
detail.hit.zdb_id:
1501537-3
Bookmarklink