FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion
Summary Type III secretion systems identified in bacterial pathogens of animals and plants transpose effectors and toxins directly into the cytosol of host cells or into the extracellular milieu. Proteins of the type III secretion apparatus are conserved among diverse and distantly related bacteria....
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| Veröffentlicht in: | Molecular microbiology 2004-07, Vol.53 (2), p.541-553 |
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| creator | Song, Y. C. Jin, S. Louie, H. Ng, D. Lau, R. Zhang, Y. Weerasekera, R. Al Rashid, S. Ward, L. A. Der, S. D. Chan, V. L. |
| description | Summary
Type III secretion systems identified in bacterial pathogens of animals and plants transpose effectors and toxins directly into the cytosol of host cells or into the extracellular milieu. Proteins of the type III secretion apparatus are conserved among diverse and distantly related bacteria. Many type III apparatus proteins have homologues in the flagellar export apparatus, supporting the notion that type III secretion systems evolved from the flagellar export apparatus. No type III secretion apparatus genes have been found in the complete genomic sequence of Campylobacter jejuni NCTC11168. In this study, we report the characterization of a protein designated FlaC of C. jejuni TGH9011. FlaC is homologous to the N‐ and C‐terminus of the C. jejuni flagellin proteins, FlaA and FlaB, but lacks the central portion of these proteins. flaC null mutants form a morphologically normal flagellum and are highly motile. In wild‐type C. jejuni cultures, FlaC is found predominantly in the extracellular milieu as a secreted protein. Null mutants of the flagellar basal rod gene (flgF) and hook gene (flgE) do not secrete FlaC, suggesting that a functional flagellar export apparatus is required for FlaC secretion. During C. jejuni infection in vitro, secreted FlaC and purified recombinant FlaC bind to HEp‐2 cells. Invasion of HEp‐2 cells by flaC null mutants was reduced to a level of 14% compared with wild type, suggesting that FlaC plays an important role in cell invasion. |
| doi_str_mv | 10.1111/j.1365-2958.2004.04175.x |
| format | Article |
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Type III secretion systems identified in bacterial pathogens of animals and plants transpose effectors and toxins directly into the cytosol of host cells or into the extracellular milieu. Proteins of the type III secretion apparatus are conserved among diverse and distantly related bacteria. Many type III apparatus proteins have homologues in the flagellar export apparatus, supporting the notion that type III secretion systems evolved from the flagellar export apparatus. No type III secretion apparatus genes have been found in the complete genomic sequence of Campylobacter jejuni NCTC11168. In this study, we report the characterization of a protein designated FlaC of C. jejuni TGH9011. FlaC is homologous to the N‐ and C‐terminus of the C. jejuni flagellin proteins, FlaA and FlaB, but lacks the central portion of these proteins. flaC null mutants form a morphologically normal flagellum and are highly motile. In wild‐type C. jejuni cultures, FlaC is found predominantly in the extracellular milieu as a secreted protein. Null mutants of the flagellar basal rod gene (flgF) and hook gene (flgE) do not secrete FlaC, suggesting that a functional flagellar export apparatus is required for FlaC secretion. During C. jejuni infection in vitro, secreted FlaC and purified recombinant FlaC bind to HEp‐2 cells. Invasion of HEp‐2 cells by flaC null mutants was reduced to a level of 14% compared with wild type, suggesting that FlaC plays an important role in cell invasion.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2004.04175.x</identifier><identifier>PMID: 15228533</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Bacterial Adhesion - genetics ; Bacterial Outer Membrane Proteins - genetics ; Bacterial Outer Membrane Proteins - physiology ; Bacterial Proteins - genetics ; Bacterial Proteins - physiology ; Bacteriology ; Biological and medical sciences ; Campylobacter jejuni ; Campylobacter jejuni - cytology ; Campylobacter jejuni - genetics ; Campylobacter jejuni - metabolism ; Campylobacter jejuni - pathogenicity ; Cell Line ; Cytoplasm - microbiology ; Epithelial Cells - metabolism ; Epithelial Cells - microbiology ; Flagella - physiology ; Flagella - secretion ; Flagellin - genetics ; Flagellin - metabolism ; Fundamental and applied biological sciences. Psychology ; Gene Deletion ; Genes, Bacterial ; Humans ; Microbiology ; Miscellaneous ; Movement ; Mutagenesis ; Protein Transport ; Sequence Homology, Amino Acid</subject><ispartof>Molecular microbiology, 2004-07, Vol.53 (2), p.541-553</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Blackwell Scientific Publications Ltd. Jul 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5695-c76b025d4dd00b4e82576ef8c2571f8540e5102e130455ae8f49e3a06f54d50f3</citedby><cites>FETCH-LOGICAL-c5695-c76b025d4dd00b4e82576ef8c2571f8540e5102e130455ae8f49e3a06f54d50f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1365-2958.2004.04175.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2004.04175.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15946005$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15228533$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Song, Y. C.</creatorcontrib><creatorcontrib>Jin, S.</creatorcontrib><creatorcontrib>Louie, H.</creatorcontrib><creatorcontrib>Ng, D.</creatorcontrib><creatorcontrib>Lau, R.</creatorcontrib><creatorcontrib>Zhang, Y.</creatorcontrib><creatorcontrib>Weerasekera, R.</creatorcontrib><creatorcontrib>Al Rashid, S.</creatorcontrib><creatorcontrib>Ward, L. A.</creatorcontrib><creatorcontrib>Der, S. D.</creatorcontrib><creatorcontrib>Chan, V. L.</creatorcontrib><title>FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Type III secretion systems identified in bacterial pathogens of animals and plants transpose effectors and toxins directly into the cytosol of host cells or into the extracellular milieu. Proteins of the type III secretion apparatus are conserved among diverse and distantly related bacteria. Many type III apparatus proteins have homologues in the flagellar export apparatus, supporting the notion that type III secretion systems evolved from the flagellar export apparatus. No type III secretion apparatus genes have been found in the complete genomic sequence of Campylobacter jejuni NCTC11168. In this study, we report the characterization of a protein designated FlaC of C. jejuni TGH9011. FlaC is homologous to the N‐ and C‐terminus of the C. jejuni flagellin proteins, FlaA and FlaB, but lacks the central portion of these proteins. flaC null mutants form a morphologically normal flagellum and are highly motile. In wild‐type C. jejuni cultures, FlaC is found predominantly in the extracellular milieu as a secreted protein. Null mutants of the flagellar basal rod gene (flgF) and hook gene (flgE) do not secrete FlaC, suggesting that a functional flagellar export apparatus is required for FlaC secretion. During C. jejuni infection in vitro, secreted FlaC and purified recombinant FlaC bind to HEp‐2 cells. Invasion of HEp‐2 cells by flaC null mutants was reduced to a level of 14% compared with wild type, suggesting that FlaC plays an important role in cell invasion.</description><subject>Bacterial Adhesion - genetics</subject><subject>Bacterial Outer Membrane Proteins - genetics</subject><subject>Bacterial Outer Membrane Proteins - physiology</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - physiology</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Campylobacter jejuni</subject><subject>Campylobacter jejuni - cytology</subject><subject>Campylobacter jejuni - genetics</subject><subject>Campylobacter jejuni - metabolism</subject><subject>Campylobacter jejuni - pathogenicity</subject><subject>Cell Line</subject><subject>Cytoplasm - microbiology</subject><subject>Epithelial Cells - metabolism</subject><subject>Epithelial Cells - microbiology</subject><subject>Flagella - physiology</subject><subject>Flagella - secretion</subject><subject>Flagellin - genetics</subject><subject>Flagellin - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Deletion</subject><subject>Genes, Bacterial</subject><subject>Humans</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Movement</subject><subject>Mutagenesis</subject><subject>Protein Transport</subject><subject>Sequence Homology, Amino Acid</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1u1DAUhS0EotPCKyALCQRSE-zYziSLLqqI_kit2AwSO8txrltHHifYCXQepW-L0xkBYoU3xz_fvTrXByFMSU7T-tTnlJUiK2pR5QUhPCecrkX-8Aytfj88RytSC5Kxqvh2hI5j7AmhjJTsJTqioigqwdgKPV441ZxihccwTGA9Hgxu1HbcuaFVeoKAe-hnb_Hm8qomlOIP55um4Ywz-hFH0AEm6PB0H4b57j4pYOPUHTinAlbjqIKa5niKW-u7iGG0iXBWOawTErHyHbbeuBm8hvh0mc4_VLSDf4VeGOUivD7oCfp68XnTXGU3Xy6vm_ObTIuyFplely0pRMe7jpCWQ1WIdQmm0kmpqQQnICgpII3OhVBQGV4DU6Q0gneCGHaC3u_7ph_4PkOc5NbGxYnyMMxR0iqNvaY8gW__AfthDj55k7QuBeUFLRNU7SEdhhgDGDkGu1VhJymRS3ayl0tEcolILtnJp-zkQyp9c-g_t1vo_hQewkrAuwOgolbOBOW1jX9xNS8JEYk723M_rYPdfxuQt7fXy479AiQwsyg</recordid><startdate>200407</startdate><enddate>200407</enddate><creator>Song, Y. C.</creator><creator>Jin, S.</creator><creator>Louie, H.</creator><creator>Ng, D.</creator><creator>Lau, R.</creator><creator>Zhang, Y.</creator><creator>Weerasekera, R.</creator><creator>Al Rashid, S.</creator><creator>Ward, L. A.</creator><creator>Der, S. D.</creator><creator>Chan, V. L.</creator><general>Blackwell Science Ltd</general><general>Blackwell Science</general><general>Blackwell Publishing Ltd</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200407</creationdate><title>FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion</title><author>Song, Y. C. ; Jin, S. ; Louie, H. ; Ng, D. ; Lau, R. ; Zhang, Y. ; Weerasekera, R. ; Al Rashid, S. ; Ward, L. A. ; Der, S. D. ; Chan, V. 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Psychology</topic><topic>Gene Deletion</topic><topic>Genes, Bacterial</topic><topic>Humans</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Movement</topic><topic>Mutagenesis</topic><topic>Protein Transport</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Song, Y. C.</creatorcontrib><creatorcontrib>Jin, S.</creatorcontrib><creatorcontrib>Louie, H.</creatorcontrib><creatorcontrib>Ng, D.</creatorcontrib><creatorcontrib>Lau, R.</creatorcontrib><creatorcontrib>Zhang, Y.</creatorcontrib><creatorcontrib>Weerasekera, R.</creatorcontrib><creatorcontrib>Al Rashid, S.</creatorcontrib><creatorcontrib>Ward, L. A.</creatorcontrib><creatorcontrib>Der, S. D.</creatorcontrib><creatorcontrib>Chan, V. L.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Song, Y. C.</au><au>Jin, S.</au><au>Louie, H.</au><au>Ng, D.</au><au>Lau, R.</au><au>Zhang, Y.</au><au>Weerasekera, R.</au><au>Al Rashid, S.</au><au>Ward, L. A.</au><au>Der, S. D.</au><au>Chan, V. L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2004-07</date><risdate>2004</risdate><volume>53</volume><issue>2</issue><spage>541</spage><epage>553</epage><pages>541-553</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Type III secretion systems identified in bacterial pathogens of animals and plants transpose effectors and toxins directly into the cytosol of host cells or into the extracellular milieu. Proteins of the type III secretion apparatus are conserved among diverse and distantly related bacteria. Many type III apparatus proteins have homologues in the flagellar export apparatus, supporting the notion that type III secretion systems evolved from the flagellar export apparatus. No type III secretion apparatus genes have been found in the complete genomic sequence of Campylobacter jejuni NCTC11168. In this study, we report the characterization of a protein designated FlaC of C. jejuni TGH9011. FlaC is homologous to the N‐ and C‐terminus of the C. jejuni flagellin proteins, FlaA and FlaB, but lacks the central portion of these proteins. flaC null mutants form a morphologically normal flagellum and are highly motile. In wild‐type C. jejuni cultures, FlaC is found predominantly in the extracellular milieu as a secreted protein. Null mutants of the flagellar basal rod gene (flgF) and hook gene (flgE) do not secrete FlaC, suggesting that a functional flagellar export apparatus is required for FlaC secretion. During C. jejuni infection in vitro, secreted FlaC and purified recombinant FlaC bind to HEp‐2 cells. Invasion of HEp‐2 cells by flaC null mutants was reduced to a level of 14% compared with wild type, suggesting that FlaC plays an important role in cell invasion.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>15228533</pmid><doi>10.1111/j.1365-2958.2004.04175.x</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular microbiology, 2004-07, Vol.53 (2), p.541-553 |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Bacterial Adhesion - genetics Bacterial Outer Membrane Proteins - genetics Bacterial Outer Membrane Proteins - physiology Bacterial Proteins - genetics Bacterial Proteins - physiology Bacteriology Biological and medical sciences Campylobacter jejuni Campylobacter jejuni - cytology Campylobacter jejuni - genetics Campylobacter jejuni - metabolism Campylobacter jejuni - pathogenicity Cell Line Cytoplasm - microbiology Epithelial Cells - metabolism Epithelial Cells - microbiology Flagella - physiology Flagella - secretion Flagellin - genetics Flagellin - metabolism Fundamental and applied biological sciences. Psychology Gene Deletion Genes, Bacterial Humans Microbiology Miscellaneous Movement Mutagenesis Protein Transport Sequence Homology, Amino Acid |
| title | FlaC, a protein of Campylobacter jejuni TGH9011 (ATCC43431) secreted through the flagellar apparatus, binds epithelial cells and influences cell invasion |
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