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Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC
Enterohaemorrhagic E. coli (EHEC) O157:H7 is a primary food-borne bacterial pathogen capable of causing life-threatening human infections which poses a serious challenge to public health worldwide. Intimin, the bacterial outer-membrane protein, plays a key role in the initiating process of EHEC infe...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Public Library of Science
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3002965/ https://www.ncbi.nlm.nih.gov/pubmed/21179574 http://dx.doi.org/10.1371/journal.pone.0015285 |
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author | Yi, Yong Ma, Ying Gao, Feng Mao, Xuhu Peng, Hao Feng, Youjun Fan, Zheng Wang, Guihua Guo, Gang Yan, Jinghua Zeng, Hao Zou, Quanming Gao, George F. |
author_facet | Yi, Yong Ma, Ying Gao, Feng Mao, Xuhu Peng, Hao Feng, Youjun Fan, Zheng Wang, Guihua Guo, Gang Yan, Jinghua Zeng, Hao Zou, Quanming Gao, George F. |
author_sort | Yi, Yong |
collection | PubMed |
description | Enterohaemorrhagic E. coli (EHEC) O157:H7 is a primary food-borne bacterial pathogen capable of causing life-threatening human infections which poses a serious challenge to public health worldwide. Intimin, the bacterial outer-membrane protein, plays a key role in the initiating process of EHEC infection. This activity is dependent upon translocation of the intimin receptor (Tir), the intimin binding partner of the bacteria-encoded host cell surface protein. Intimin has attracted considerable attention due to its potential function as an antibacterial drug target. Here, we report the crystal structure of the Tir-binding domain of intimin (Int188) from E. coli O157:H7 at 2.8 Å resolution, together with a mutant (IntN916Y) at 2.6 Å. We also built the structural model of EHEC intimin-Tir complex and analyzed the key binding residues. It suggested that the binding pattern of intimin and Tir between EHEC and Enteropathogenic E. coli (EPEC) adopt a similar mode and they can complement with each other. Detailed structural comparison indicates that there are four major points of structural variations between EHEC and EPEC intimins: one in Domain I (Ig-like domain), the other three located in Domain II (C-type lectin-like domain). These variations result in different binding affinities. These findings provide structural insight into the binding pattern of intimin to Tir and the molecular mechanism of EHEC O157: H7. |
format | Text |
id | pubmed-3002965 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-30029652010-12-21 Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC Yi, Yong Ma, Ying Gao, Feng Mao, Xuhu Peng, Hao Feng, Youjun Fan, Zheng Wang, Guihua Guo, Gang Yan, Jinghua Zeng, Hao Zou, Quanming Gao, George F. PLoS One Research Article Enterohaemorrhagic E. coli (EHEC) O157:H7 is a primary food-borne bacterial pathogen capable of causing life-threatening human infections which poses a serious challenge to public health worldwide. Intimin, the bacterial outer-membrane protein, plays a key role in the initiating process of EHEC infection. This activity is dependent upon translocation of the intimin receptor (Tir), the intimin binding partner of the bacteria-encoded host cell surface protein. Intimin has attracted considerable attention due to its potential function as an antibacterial drug target. Here, we report the crystal structure of the Tir-binding domain of intimin (Int188) from E. coli O157:H7 at 2.8 Å resolution, together with a mutant (IntN916Y) at 2.6 Å. We also built the structural model of EHEC intimin-Tir complex and analyzed the key binding residues. It suggested that the binding pattern of intimin and Tir between EHEC and Enteropathogenic E. coli (EPEC) adopt a similar mode and they can complement with each other. Detailed structural comparison indicates that there are four major points of structural variations between EHEC and EPEC intimins: one in Domain I (Ig-like domain), the other three located in Domain II (C-type lectin-like domain). These variations result in different binding affinities. These findings provide structural insight into the binding pattern of intimin to Tir and the molecular mechanism of EHEC O157: H7. Public Library of Science 2010-12-16 /pmc/articles/PMC3002965/ /pubmed/21179574 http://dx.doi.org/10.1371/journal.pone.0015285 Text en Yi et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Yi, Yong Ma, Ying Gao, Feng Mao, Xuhu Peng, Hao Feng, Youjun Fan, Zheng Wang, Guihua Guo, Gang Yan, Jinghua Zeng, Hao Zou, Quanming Gao, George F. Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title | Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title_full | Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title_fullStr | Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title_full_unstemmed | Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title_short | Crystal Structure of EHEC Intimin: Insights into the Complementarity between EPEC and EHEC |
title_sort | crystal structure of ehec intimin: insights into the complementarity between epec and ehec |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3002965/ https://www.ncbi.nlm.nih.gov/pubmed/21179574 http://dx.doi.org/10.1371/journal.pone.0015285 |
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