HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it>
<p>Abstract</p> <p>Background</p> <p>Acute gastroenteritis caused by the food-borne pathogen <it>Campylobacter jejuni </it>is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In <it>C. jej...
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| Format: | Article |
| Language: | English |
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BMC
2011-09-01
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| Series: | Gut Pathogens |
| Subjects: | |
| Online Access: | http://www.gutpathogens.com/content/3/1/13 |
| _version_ | 1818825495559536640 |
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| author | Bæk Kristoffer T Vegge Christina S Brøndsted Lone |
| author_facet | Bæk Kristoffer T Vegge Christina S Brøndsted Lone |
| author_sort | Bæk Kristoffer T |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Acute gastroenteritis caused by the food-borne pathogen <it>Campylobacter jejuni </it>is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In <it>C. jejuni</it>, the periplasmic protein HtrA is required for efficient binding to epithelial cells. HtrA has both protease and chaperone activity, and is important for virulence of several bacterial pathogens.</p> <p>Results</p> <p>The aim of this study was to determine the role of the dual activities of HtrA in host cell interaction of <it>C. jejuni </it>by comparing an <it>htrA </it>mutant lacking protease activity, but retaining chaperone activity, with a Δ<it>htrA </it>mutant and the wild type strain. Binding of <it>C</it>. <it>jejuni </it>to both epithelial cells and macrophages was facilitated mainly by HtrA chaperone activity that may be involved in folding of outer membrane adhesins. In contrast, HtrA protease activity played only a minor role in interaction with host cells.</p> <p>Conclusion</p> <p>We show that HtrA protease and chaperone activities contribute differently to <it>C. jejuni</it>'s interaction with mammalian host cells, with the chaperone activity playing the major role in host cell binding.</p> |
| first_indexed | 2024-12-19T00:12:41Z |
| format | Article |
| id | doaj.art-f239a7f86fc04e41b11548d42fe366e5 |
| institution | Directory Open Access Journal |
| issn | 1757-4749 |
| language | English |
| last_indexed | 2024-12-19T00:12:41Z |
| publishDate | 2011-09-01 |
| publisher | BMC |
| record_format | Article |
| series | Gut Pathogens |
| spelling | doaj.art-f239a7f86fc04e41b11548d42fe366e52022-12-21T20:45:59ZengBMCGut Pathogens1757-47492011-09-01311310.1186/1757-4749-3-13HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it>Bæk Kristoffer TVegge Christina SBrøndsted Lone<p>Abstract</p> <p>Background</p> <p>Acute gastroenteritis caused by the food-borne pathogen <it>Campylobacter jejuni </it>is associated with attachment of bacteria to the intestinal epithelium and subsequent invasion of epithelial cells. In <it>C. jejuni</it>, the periplasmic protein HtrA is required for efficient binding to epithelial cells. HtrA has both protease and chaperone activity, and is important for virulence of several bacterial pathogens.</p> <p>Results</p> <p>The aim of this study was to determine the role of the dual activities of HtrA in host cell interaction of <it>C. jejuni </it>by comparing an <it>htrA </it>mutant lacking protease activity, but retaining chaperone activity, with a Δ<it>htrA </it>mutant and the wild type strain. Binding of <it>C</it>. <it>jejuni </it>to both epithelial cells and macrophages was facilitated mainly by HtrA chaperone activity that may be involved in folding of outer membrane adhesins. In contrast, HtrA protease activity played only a minor role in interaction with host cells.</p> <p>Conclusion</p> <p>We show that HtrA protease and chaperone activities contribute differently to <it>C. jejuni</it>'s interaction with mammalian host cells, with the chaperone activity playing the major role in host cell binding.</p>http://www.gutpathogens.com/content/3/1/13HtrAchaperoneprotease<it>Campylobacter jejuni</it>INT-407phagocytosisvirulence |
| spellingShingle | Bæk Kristoffer T Vegge Christina S Brøndsted Lone HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> Gut Pathogens HtrA chaperone protease <it>Campylobacter jejuni</it> INT-407 phagocytosis virulence |
| title | HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> |
| title_full | HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> |
| title_fullStr | HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> |
| title_full_unstemmed | HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> |
| title_short | HtrA chaperone activity contributes to host cell binding in <it>Campylobacter jejuni</it> |
| title_sort | htra chaperone activity contributes to host cell binding in it campylobacter jejuni it |
| topic | HtrA chaperone protease <it>Campylobacter jejuni</it> INT-407 phagocytosis virulence |
| url | http://www.gutpathogens.com/content/3/1/13 |
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