Protein interactions and regulation of EscA in enterohemorrhagic E. coli.
Infections caused by enterohemorrhagic Escherichia coli (EHEC) can lead to diarrhea with abdominal cramps and sometimes are complicated by severe hemolytic uremic syndrome. EHEC secretes effector proteins into host cells through a type III secretion system that is composed of proteins encoded by a c...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3890302?pdf=render |
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| author | Ching-Nan Lin Wei-Sheng W Sun Hui-Yin Lu Swee-Chuan Ng Ying-Shu Liao Wan-Jr Syu |
| author_facet | Ching-Nan Lin Wei-Sheng W Sun Hui-Yin Lu Swee-Chuan Ng Ying-Shu Liao Wan-Jr Syu |
| author_sort | Ching-Nan Lin |
| collection | DOAJ |
| description | Infections caused by enterohemorrhagic Escherichia coli (EHEC) can lead to diarrhea with abdominal cramps and sometimes are complicated by severe hemolytic uremic syndrome. EHEC secretes effector proteins into host cells through a type III secretion system that is composed of proteins encoded by a chromosomal island, locus for the enterocyte effacement (LEE). EspA is the major component of the filamentous structure connecting the bacteria and the host's cells. Synthesis and secretion of EspA must be carefully controlled since the protein is prone to polymerize. CesAB, CesA2, and EscL have been identified as being able to interact with EspA. Furthermore, the intracellular level of EspA declines when cesAB, cesA2, and escL are individually deleted. Here, we report a LEE gene named l0033, which also affects the intracellular level of EspA. We renamed l0033 as escA since its counterpart in enteropathogenic E. coli has been recently described. Similar to CesAB, EscL, and CesA2, EscA interacts with EspA and enhances the protein stability of EspA. However, EscA is also able to interact with inner membrane-associated EscL, CesA2, and EscN, but not with cytoplasmic CesAB. In terms of gene organizations, escA locates in LEE3. Expression of EscA is faithfully regulated via Mpc, the first gene product of LEE3. Since Mpc is tightly regulated to low level, we suggest that EscA is highly synchronized and critical to the process of escorting EspA to its final destination. |
| first_indexed | 2024-12-11T01:22:47Z |
| format | Article |
| id | doaj.art-34933b6f9adb4795bac9dac7fe900825 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T01:22:47Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-34933b6f9adb4795bac9dac7fe9008252022-12-22T01:25:38ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0191e8535410.1371/journal.pone.0085354Protein interactions and regulation of EscA in enterohemorrhagic E. coli.Ching-Nan LinWei-Sheng W SunHui-Yin LuSwee-Chuan NgYing-Shu LiaoWan-Jr SyuInfections caused by enterohemorrhagic Escherichia coli (EHEC) can lead to diarrhea with abdominal cramps and sometimes are complicated by severe hemolytic uremic syndrome. EHEC secretes effector proteins into host cells through a type III secretion system that is composed of proteins encoded by a chromosomal island, locus for the enterocyte effacement (LEE). EspA is the major component of the filamentous structure connecting the bacteria and the host's cells. Synthesis and secretion of EspA must be carefully controlled since the protein is prone to polymerize. CesAB, CesA2, and EscL have been identified as being able to interact with EspA. Furthermore, the intracellular level of EspA declines when cesAB, cesA2, and escL are individually deleted. Here, we report a LEE gene named l0033, which also affects the intracellular level of EspA. We renamed l0033 as escA since its counterpart in enteropathogenic E. coli has been recently described. Similar to CesAB, EscL, and CesA2, EscA interacts with EspA and enhances the protein stability of EspA. However, EscA is also able to interact with inner membrane-associated EscL, CesA2, and EscN, but not with cytoplasmic CesAB. In terms of gene organizations, escA locates in LEE3. Expression of EscA is faithfully regulated via Mpc, the first gene product of LEE3. Since Mpc is tightly regulated to low level, we suggest that EscA is highly synchronized and critical to the process of escorting EspA to its final destination.http://europepmc.org/articles/PMC3890302?pdf=render |
| spellingShingle | Ching-Nan Lin Wei-Sheng W Sun Hui-Yin Lu Swee-Chuan Ng Ying-Shu Liao Wan-Jr Syu Protein interactions and regulation of EscA in enterohemorrhagic E. coli. PLoS ONE |
| title | Protein interactions and regulation of EscA in enterohemorrhagic E. coli. |
| title_full | Protein interactions and regulation of EscA in enterohemorrhagic E. coli. |
| title_fullStr | Protein interactions and regulation of EscA in enterohemorrhagic E. coli. |
| title_full_unstemmed | Protein interactions and regulation of EscA in enterohemorrhagic E. coli. |
| title_short | Protein interactions and regulation of EscA in enterohemorrhagic E. coli. |
| title_sort | protein interactions and regulation of esca in enterohemorrhagic e coli |
| url | http://europepmc.org/articles/PMC3890302?pdf=render |
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