A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion

<p>Abstract</p> <p>Open reading frame <it>l0045 </it>in the pathogenic island of enterohemorrhagic <it>Escherichia coli </it>O157:H7 has been predicted to encode a lytic transglycosylase that is homologous to two different gene products encoded by the same b...

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Main Authors: Hu Wensi S, Ng Swee-Chuan, Wang Shao-Hung, Lin Ching-Nan, Yu Yen-Chi, Syu Wan-Jr
Format: Article
Language:English
Published: BMC 2010-06-01
Series:Journal of Biomedical Science
Online Access:http://www.jbiomedsci.com/content/17/1/52
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spelling doaj-8ee2686a76874738a33f2ec4e4ac82dc2020-11-24T20:48:01ZengBMCJournal of Biomedical Science1021-77701423-01272010-06-011715210.1186/1423-0127-17-52A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretionHu Wensi SNg Swee-ChuanWang Shao-HungLin Ching-NanYu Yen-ChiSyu Wan-Jr<p>Abstract</p> <p>Open reading frame <it>l0045 </it>in the pathogenic island of enterohemorrhagic <it>Escherichia coli </it>O157:H7 has been predicted to encode a lytic transglycosylase that is homologous to two different gene products encoded by the same bacteria at loci away from the island. To deduce the necessity of the presence in the island, we created an <it>l0045-</it>deleted strain of EHEC and observed that both the level of cytosolic EspA and that of the other type III secreted proteins in the media were affected. In a complementation assay, a low level-expressing L0045 appeared to recover efficiently the type III secretion (TTS). On the other hand, when <it>l0045 </it>was driven to express robustly, the intracellular levels of representative TTS proteins were severely suppressed. This suppression is apparently caused by the protein of L0045 <it>per se </it>since introducing an early translational termination codon abolished the suppression. Intriguingly, the authentic L0045 was hardly detected in all lysates of EHEC differently prepared while the same construct was expectedly expressed in the K-12 strain. A unique network must exist in EHEC to tightly regulate the presence of L0045, and we found that a LEE regulator (GrlA) is critically involved in this regulation.</p> http://www.jbiomedsci.com/content/17/1/52
collection DOAJ
language English
format Article
sources DOAJ
author Hu Wensi S
Ng Swee-Chuan
Wang Shao-Hung
Lin Ching-Nan
Yu Yen-Chi
Syu Wan-Jr
spellingShingle Hu Wensi S
Ng Swee-Chuan
Wang Shao-Hung
Lin Ching-Nan
Yu Yen-Chi
Syu Wan-Jr
A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
Journal of Biomedical Science
author_facet Hu Wensi S
Ng Swee-Chuan
Wang Shao-Hung
Lin Ching-Nan
Yu Yen-Chi
Syu Wan-Jr
author_sort Hu Wensi S
title A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
title_short A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
title_full A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
title_fullStr A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
title_full_unstemmed A putative lytic transglycosylase tightly regulated and critical for the EHEC type three secretion
title_sort putative lytic transglycosylase tightly regulated and critical for the ehec type three secretion
publisher BMC
series Journal of Biomedical Science
issn 1021-7770
1423-0127
publishDate 2010-06-01
description <p>Abstract</p> <p>Open reading frame <it>l0045 </it>in the pathogenic island of enterohemorrhagic <it>Escherichia coli </it>O157:H7 has been predicted to encode a lytic transglycosylase that is homologous to two different gene products encoded by the same bacteria at loci away from the island. To deduce the necessity of the presence in the island, we created an <it>l0045-</it>deleted strain of EHEC and observed that both the level of cytosolic EspA and that of the other type III secreted proteins in the media were affected. In a complementation assay, a low level-expressing L0045 appeared to recover efficiently the type III secretion (TTS). On the other hand, when <it>l0045 </it>was driven to express robustly, the intracellular levels of representative TTS proteins were severely suppressed. This suppression is apparently caused by the protein of L0045 <it>per se </it>since introducing an early translational termination codon abolished the suppression. Intriguingly, the authentic L0045 was hardly detected in all lysates of EHEC differently prepared while the same construct was expectedly expressed in the K-12 strain. A unique network must exist in EHEC to tightly regulate the presence of L0045, and we found that a LEE regulator (GrlA) is critically involved in this regulation.</p>
url http://www.jbiomedsci.com/content/17/1/52
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