Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/55469
DC Field | Value | Language |
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dc.contributor | Department of Applied Biology and Chemical Technology | - |
dc.creator | Liu, M | - |
dc.creator | Chen, S | - |
dc.date.accessioned | 2016-09-07T02:21:54Z | - |
dc.date.available | 2016-09-07T02:21:54Z | - |
dc.identifier.uri | http://hdl.handle.net/10397/55469 | - |
dc.language.iso | en | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.rights | This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.rights | The following publication Liu, M. and Chen, S. A novel adhesive factor contributing to the virulence of Vibrio parahaemolyticus. Sci. Rep. 5, 14449 (2015) is available at https://dx.doi.org/10.1038/srep14449 | en_US |
dc.title | A novel adhesive factor contributing to the virulence of vibrio parahaemolyticus | en_US |
dc.type | Journal/Magazine Article | en_US |
dc.identifier.volume | 5 | - |
dc.identifier.doi | 10.1038/srep14449 | - |
dcterms.abstract | Bacterial adhesins play a pivotal role in the tight bacteria-host cells attachment to initiate the downstream processes and bacterial infection of hosts. In this study, we identified a novel adhesin, VpadF in V. parahaemolyticus. Deletion of VpadF in V. parahaemolyticus markedly impaired its attachment and cytotoxicity to epithelial cells, as well as attenuated the virulence in murine model. Biochemical studies revealed that VpadF recognized both fibronectin and fibrinogen. The binding of VpadF to these two host receptors was mainly dependent on the its fifth bacterial immunoglobulin-like group domain and its C-Terminal tail. Our finding suggested that VpadF is a major virulence factor of V. parahaemolyticus and a potential good candidate for V. parahaemolyticus infection control for both vaccine development and drug target. | - |
dcterms.accessRights | open access | en_US |
dcterms.bibliographicCitation | Scientific reports, 24 2015, v. 5, no. , p. 1-10 | - |
dcterms.isPartOf | Scientific reports | - |
dcterms.issued | 2015 | - |
dc.identifier.scopus | 2-s2.0-84942155004 | - |
dc.identifier.eissn | 2045-2322 | - |
dc.identifier.rosgroupid | 2015001046 | - |
dc.description.ros | 2015-2016 > Academic research: refereed > Publication in refereed journal | - |
dc.description.oa | Version of Record | en_US |
dc.identifier.FolderNumber | OA_IR/PIRA | en_US |
dc.description.pubStatus | Published | en_US |
Appears in Collections: | Journal/Magazine Article |
Files in This Item:
File | Description | Size | Format | |
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Liu_Virulence_Vibrio_Parahaemolyticus.pdf | 1.23 MB | Adobe PDF | View/Open |
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