Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells
Campylobacter jejuni is the most frequent cause of severe gastroenteritis in the developed world. The major symptom of campylobacteriosis is inflammatory diarrhoea. The molecular mechanisms of this infection are poorly understood compared to those of less frequent disease-causing pathogens. In a pre...
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description | Campylobacter jejuni is the most frequent cause of severe gastroenteritis in the developed world. The major symptom of campylobacteriosis is inflammatory diarrhoea. The molecular mechanisms of this infection are poorly understood compared to those of less frequent disease-causing pathogens. In a previous study, we identified C. jejuni proteins that antibodies in human campylobacteriosis patients reacted with. One of the immunogenic proteins identified (Cj0917) displays homology to carbon starvation protein A (CstA) from Escherichia coli, where this protein is involved in the starvation response and peptide uptake. In contrast to many bacteria, C. jejuni relies on amino acids and organic acids for energy, but in vivo it is highly likely that peptides are also utilized, although their mechanisms of uptake are unknown. In this study, Biolog phenotype microarrays have been used to show that a ΔcstA mutant has a reduced ability to utilize a number of di- and tri-peptides as nitrogen sources. This phenotype was restored through genetic complementation, suggesting CstA is a peptide uptake system in C. jejuni. Furthermore, the ΔcstA mutant also displayed reduced motility and reduced agglutination compared to WT bacteria; these phenotypes were also restored through complementation. Murine dendritic cells exposed to UV-killed bacteria showed a reduced IL-12 production, but the same IL-10 response when encountering C. jejuni ΔcstA compared to the WT strain. The greater Th1 stimulation elicited by the WT as compared to ΔcstA mutant cells indicates an altered antigenic presentation on the surface, and thus an altered recognition of the mutant. Thus, we conclude that C. jejuni CstA is important not only for peptide utilization, but also it may influence host-pathogen interactions. |
doi_str_mv | 10.1099/jmm.0.059345-0 |
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J ; VEGGE, C. S ; FRØKIÆR, H ; HOWLETT, R. M ; KROGFELT, K. A ; KELLY, D. J ; INGMER, H</creator><creatorcontrib>RASMUSSEN, J. J ; VEGGE, C. S ; FRØKIÆR, H ; HOWLETT, R. M ; KROGFELT, K. A ; KELLY, D. J ; INGMER, H</creatorcontrib><description>Campylobacter jejuni is the most frequent cause of severe gastroenteritis in the developed world. The major symptom of campylobacteriosis is inflammatory diarrhoea. The molecular mechanisms of this infection are poorly understood compared to those of less frequent disease-causing pathogens. In a previous study, we identified C. jejuni proteins that antibodies in human campylobacteriosis patients reacted with. One of the immunogenic proteins identified (Cj0917) displays homology to carbon starvation protein A (CstA) from Escherichia coli, where this protein is involved in the starvation response and peptide uptake. In contrast to many bacteria, C. jejuni relies on amino acids and organic acids for energy, but in vivo it is highly likely that peptides are also utilized, although their mechanisms of uptake are unknown. In this study, Biolog phenotype microarrays have been used to show that a ΔcstA mutant has a reduced ability to utilize a number of di- and tri-peptides as nitrogen sources. This phenotype was restored through genetic complementation, suggesting CstA is a peptide uptake system in C. jejuni. Furthermore, the ΔcstA mutant also displayed reduced motility and reduced agglutination compared to WT bacteria; these phenotypes were also restored through complementation. Murine dendritic cells exposed to UV-killed bacteria showed a reduced IL-12 production, but the same IL-10 response when encountering C. jejuni ΔcstA compared to the WT strain. The greater Th1 stimulation elicited by the WT as compared to ΔcstA mutant cells indicates an altered antigenic presentation on the surface, and thus an altered recognition of the mutant. Thus, we conclude that C. jejuni CstA is important not only for peptide utilization, but also it may influence host-pathogen interactions.</description><identifier>ISSN: 0022-2615</identifier><identifier>EISSN: 1473-5644</identifier><identifier>DOI: 10.1099/jmm.0.059345-0</identifier><identifier>PMID: 23682166</identifier><identifier>CODEN: JMMIAV</identifier><language>eng</language><publisher>Reading: Society for General Microbiology</publisher><subject>Agglutination ; Amino Acid Sequence ; Animals ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Campylobacter Infections - immunology ; Campylobacter Infections - microbiology ; Campylobacter jejuni - genetics ; Campylobacter jejuni - immunology ; Campylobacter jejuni - physiology ; Carbon - metabolism ; Dendritic Cells - immunology ; Dendritic Cells - microbiology ; Dipeptides - metabolism ; Female ; Fundamental and applied biological sciences. Psychology ; Genetic Complementation Test ; Host-Pathogen Interactions - immunology ; Humans ; Infectious diseases ; Interleukin-12 - analysis ; Interleukin-12 - immunology ; Medical sciences ; Mice ; Mice, Inbred C57BL ; Microbiology ; Miscellaneous ; Molecular Sequence Data ; Nitrogen - metabolism ; Phenotype ; Phylogeny ; Sequence Alignment ; Sequence Deletion</subject><ispartof>Journal of medical microbiology, 2013-08, Vol.62 (8), p.1135-1143</ispartof><rights>2014 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-1f10d4667ec04720a87b148801afc802d290fc9d0adf1f921bc63687487e96233</citedby><cites>FETCH-LOGICAL-c391t-1f10d4667ec04720a87b148801afc802d290fc9d0adf1f921bc63687487e96233</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,3735,27911,27912</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=27632426$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23682166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>RASMUSSEN, J. J</creatorcontrib><creatorcontrib>VEGGE, C. S</creatorcontrib><creatorcontrib>FRØKIÆR, H</creatorcontrib><creatorcontrib>HOWLETT, R. M</creatorcontrib><creatorcontrib>KROGFELT, K. A</creatorcontrib><creatorcontrib>KELLY, D. J</creatorcontrib><creatorcontrib>INGMER, H</creatorcontrib><title>Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells</title><title>Journal of medical microbiology</title><addtitle>J Med Microbiol</addtitle><description>Campylobacter jejuni is the most frequent cause of severe gastroenteritis in the developed world. The major symptom of campylobacteriosis is inflammatory diarrhoea. The molecular mechanisms of this infection are poorly understood compared to those of less frequent disease-causing pathogens. In a previous study, we identified C. jejuni proteins that antibodies in human campylobacteriosis patients reacted with. One of the immunogenic proteins identified (Cj0917) displays homology to carbon starvation protein A (CstA) from Escherichia coli, where this protein is involved in the starvation response and peptide uptake. In contrast to many bacteria, C. jejuni relies on amino acids and organic acids for energy, but in vivo it is highly likely that peptides are also utilized, although their mechanisms of uptake are unknown. In this study, Biolog phenotype microarrays have been used to show that a ΔcstA mutant has a reduced ability to utilize a number of di- and tri-peptides as nitrogen sources. This phenotype was restored through genetic complementation, suggesting CstA is a peptide uptake system in C. jejuni. Furthermore, the ΔcstA mutant also displayed reduced motility and reduced agglutination compared to WT bacteria; these phenotypes were also restored through complementation. Murine dendritic cells exposed to UV-killed bacteria showed a reduced IL-12 production, but the same IL-10 response when encountering C. jejuni ΔcstA compared to the WT strain. The greater Th1 stimulation elicited by the WT as compared to ΔcstA mutant cells indicates an altered antigenic presentation on the surface, and thus an altered recognition of the mutant. Thus, we conclude that C. jejuni CstA is important not only for peptide utilization, but also it may influence host-pathogen interactions.</description><subject>Agglutination</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Campylobacter Infections - immunology</subject><subject>Campylobacter Infections - microbiology</subject><subject>Campylobacter jejuni - genetics</subject><subject>Campylobacter jejuni - immunology</subject><subject>Campylobacter jejuni - physiology</subject><subject>Carbon - metabolism</subject><subject>Dendritic Cells - immunology</subject><subject>Dendritic Cells - microbiology</subject><subject>Dipeptides - metabolism</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic Complementation Test</subject><subject>Host-Pathogen Interactions - immunology</subject><subject>Humans</subject><subject>Infectious diseases</subject><subject>Interleukin-12 - analysis</subject><subject>Interleukin-12 - immunology</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular Sequence Data</subject><subject>Nitrogen - metabolism</subject><subject>Phenotype</subject><subject>Phylogeny</subject><subject>Sequence Alignment</subject><subject>Sequence Deletion</subject><issn>0022-2615</issn><issn>1473-5644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkU2PFCEQhonRuOPq1aPhYrIm9lh8DN0cJxO_kk286JnQQK9MaLoFepLxF_kzpZ1RTxTUU29R9SL0ksCWgJTvjuO4hS3sJOO7Bh6hDeEta3aC88doA0BpQwXZ3aBnOR8BSMuYfIpuKBMdJUJs0K-DHudzmHptikv46I5L9Njo1E8R56LTSRdfwzlNxfmI9_jukMv-DfYZ-3iawsnZGuDZzcVbh5fig__5p-YtHqf1Vs5YR4v1w0Oo2XjNrU_fdcYapym4VSIXPy7h0m4asHXRJl-8wcaFkJ-jJ4MO2b24nrfo24f3Xw-fmvsvHz8f9veNYZKUhgwELBeidQZ4S0F3bU941wHRg-mAWiphMNKCtgMZJCW9EXUZLe9aJwVl7BbdXXTrxD8Wl4safV5_oKOblqwIB6hcJ2VFtxfUpCnn5AY1Jz_qdFYE1OqOqu4oUBd3FNSCV1ftpR-d_Yf_taMCr6-AzkaHIelofP7PtYJRTgX7DXusmoc</recordid><startdate>20130801</startdate><enddate>20130801</enddate><creator>RASMUSSEN, J. J</creator><creator>VEGGE, C. S</creator><creator>FRØKIÆR, H</creator><creator>HOWLETT, R. M</creator><creator>KROGFELT, K. A</creator><creator>KELLY, D. J</creator><creator>INGMER, H</creator><general>Society for General Microbiology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20130801</creationdate><title>Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells</title><author>RASMUSSEN, J. J ; VEGGE, C. S ; FRØKIÆR, H ; HOWLETT, R. M ; KROGFELT, K. A ; KELLY, D. J ; INGMER, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-1f10d4667ec04720a87b148801afc802d290fc9d0adf1f921bc63687487e96233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Agglutination</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Campylobacter Infections - immunology</topic><topic>Campylobacter Infections - microbiology</topic><topic>Campylobacter jejuni - genetics</topic><topic>Campylobacter jejuni - immunology</topic><topic>Campylobacter jejuni - physiology</topic><topic>Carbon - metabolism</topic><topic>Dendritic Cells - immunology</topic><topic>Dendritic Cells - microbiology</topic><topic>Dipeptides - metabolism</topic><topic>Female</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic Complementation Test</topic><topic>Host-Pathogen Interactions - immunology</topic><topic>Humans</topic><topic>Infectious diseases</topic><topic>Interleukin-12 - analysis</topic><topic>Interleukin-12 - immunology</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular Sequence Data</topic><topic>Nitrogen - metabolism</topic><topic>Phenotype</topic><topic>Phylogeny</topic><topic>Sequence Alignment</topic><topic>Sequence Deletion</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>RASMUSSEN, J. J</creatorcontrib><creatorcontrib>VEGGE, C. S</creatorcontrib><creatorcontrib>FRØKIÆR, H</creatorcontrib><creatorcontrib>HOWLETT, R. M</creatorcontrib><creatorcontrib>KROGFELT, K. A</creatorcontrib><creatorcontrib>KELLY, D. 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J</au><au>INGMER, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells</atitle><jtitle>Journal of medical microbiology</jtitle><addtitle>J Med Microbiol</addtitle><date>2013-08-01</date><risdate>2013</risdate><volume>62</volume><issue>8</issue><spage>1135</spage><epage>1143</epage><pages>1135-1143</pages><issn>0022-2615</issn><eissn>1473-5644</eissn><coden>JMMIAV</coden><abstract>Campylobacter jejuni is the most frequent cause of severe gastroenteritis in the developed world. The major symptom of campylobacteriosis is inflammatory diarrhoea. The molecular mechanisms of this infection are poorly understood compared to those of less frequent disease-causing pathogens. In a previous study, we identified C. jejuni proteins that antibodies in human campylobacteriosis patients reacted with. One of the immunogenic proteins identified (Cj0917) displays homology to carbon starvation protein A (CstA) from Escherichia coli, where this protein is involved in the starvation response and peptide uptake. In contrast to many bacteria, C. jejuni relies on amino acids and organic acids for energy, but in vivo it is highly likely that peptides are also utilized, although their mechanisms of uptake are unknown. In this study, Biolog phenotype microarrays have been used to show that a ΔcstA mutant has a reduced ability to utilize a number of di- and tri-peptides as nitrogen sources. This phenotype was restored through genetic complementation, suggesting CstA is a peptide uptake system in C. jejuni. Furthermore, the ΔcstA mutant also displayed reduced motility and reduced agglutination compared to WT bacteria; these phenotypes were also restored through complementation. Murine dendritic cells exposed to UV-killed bacteria showed a reduced IL-12 production, but the same IL-10 response when encountering C. jejuni ΔcstA compared to the WT strain. The greater Th1 stimulation elicited by the WT as compared to ΔcstA mutant cells indicates an altered antigenic presentation on the surface, and thus an altered recognition of the mutant. Thus, we conclude that C. jejuni CstA is important not only for peptide utilization, but also it may influence host-pathogen interactions.</abstract><cop>Reading</cop><pub>Society for General Microbiology</pub><pmid>23682166</pmid><doi>10.1099/jmm.0.059345-0</doi><tpages>9</tpages></addata></record> |
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subjects | Agglutination Amino Acid Sequence Animals Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Campylobacter Infections - immunology Campylobacter Infections - microbiology Campylobacter jejuni - genetics Campylobacter jejuni - immunology Campylobacter jejuni - physiology Carbon - metabolism Dendritic Cells - immunology Dendritic Cells - microbiology Dipeptides - metabolism Female Fundamental and applied biological sciences. Psychology Genetic Complementation Test Host-Pathogen Interactions - immunology Humans Infectious diseases Interleukin-12 - analysis Interleukin-12 - immunology Medical sciences Mice Mice, Inbred C57BL Microbiology Miscellaneous Molecular Sequence Data Nitrogen - metabolism Phenotype Phylogeny Sequence Alignment Sequence Deletion |
title | Campylobacter jejuni carbon starvation protein A (CstA) is involved in peptide utilization, motility and agglutination, and has a role in stimulation of dendritic cells |
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