Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding
The virulence plasmid‐encoded YadA of Yersinia enterocolitica serotype O:3 is a 430‐amino‐acid outer membrane protein, synthesized with a 25‐amino‐acid signal peptide. YadA forms homotrimeric surface structures that function as adhesin between bacteria and collagen as well as other host proteins. Th...
Gespeichert in:
| Veröffentlicht in: | Molecular microbiology 2000-07, Vol.37 (1), p.192-206 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 206 |
|---|---|
| container_issue | 1 |
| container_start_page | 192 |
| container_title | Molecular microbiology |
| container_volume | 37 |
| creator | Tahir, Yasmin El Kuusela, Pentti Skurnik, Mikael |
| description | The virulence plasmid‐encoded YadA of Yersinia enterocolitica serotype O:3 is a 430‐amino‐acid outer membrane protein, synthesized with a 25‐amino‐acid signal peptide. YadA forms homotrimeric surface structures that function as adhesin between bacteria and collagen as well as other host proteins. The structure–function relationships of YadA were studied, and the collagen‐binding determinants of YadA were located to its amino‐terminal half. Collagen did not bind to any of the overlapping 16‐mer YadA peptides, indicating that the collagen binding site of YadA is conformational. Epitope mapping of YadA identified 12 linear antigenic epitopes altogether. Seven epitopes were uniquely recognized by an anti‐YadA antiserum able to inhibit collagen binding. Four of these epitopes shared a motif NSVAIG–S that is repeated eight times within the N‐terminal half of YadA. Site‐directed mutagenesis showed that these motifs are absolutely required for YadA‐mediated collagen binding, revealing a novel type of collagen‐binding mechanism. |
| doi_str_mv | 10.1046/j.1365-2958.2000.01992.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_17826641</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>17826641</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5012-83f97ef6256a4eccaf5e9e0554931a972142d4e137479a103a87289e042a75603</originalsourceid><addsrcrecordid>eNqNUctu1DAUtRAVHQq_gLxil-BH7CQLFqOKlpH6WLQgurLc5GbGo8Qe4kxpd_0EJH6FL-qXcN0pFUtWvtJ5WocQylnOWaE_rHMutcpErapcMMZyxuta5LcvyOwZeElmrFYsk5X4tk9ex7hmjEum5Suyz1ktueR6Rn4fbX0zueBtTwe72Ti_pKGj0wroFYzReWcp-AnG0ITeTa6x1LYrQIBe2Xae00WLsOsQSC5JC265mujZxdf54pg-3P-iF3QISIkURcnYDs6Hh_uf6IoXBq9s3_1N3YxhAiQ6fxP6G2iTCKN7uwRPr51vseEbstfZPsLbp_eAfDn6dHn4OTs5P14czk-yRjEuskp2dQmdFkrbAprGdgpqYEoV-Htbl4IXoi2Ay7Ioa8uZtFUpKmQUwpZKM3lA3u98sdT3LcTJDC42gGU8hG00vKyE1gVHYrUjNmOIcYTObEY32PHOcGbSYmZt0jAmDWPSYuZxMXOL0ndPGdvrAdp_hLuJkPBxR_jherj7b2NzerpIl_wDpCmoOw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>17826641</pqid></control><display><type>article</type><title>Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding</title><source>MEDLINE</source><source>Wiley Free Content</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library All Journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Tahir, Yasmin El ; Kuusela, Pentti ; Skurnik, Mikael</creator><creatorcontrib>Tahir, Yasmin El ; Kuusela, Pentti ; Skurnik, Mikael</creatorcontrib><description>The virulence plasmid‐encoded YadA of Yersinia enterocolitica serotype O:3 is a 430‐amino‐acid outer membrane protein, synthesized with a 25‐amino‐acid signal peptide. YadA forms homotrimeric surface structures that function as adhesin between bacteria and collagen as well as other host proteins. The structure–function relationships of YadA were studied, and the collagen‐binding determinants of YadA were located to its amino‐terminal half. Collagen did not bind to any of the overlapping 16‐mer YadA peptides, indicating that the collagen binding site of YadA is conformational. Epitope mapping of YadA identified 12 linear antigenic epitopes altogether. Seven epitopes were uniquely recognized by an anti‐YadA antiserum able to inhibit collagen binding. Four of these epitopes shared a motif NSVAIG–S that is repeated eight times within the N‐terminal half of YadA. Site‐directed mutagenesis showed that these motifs are absolutely required for YadA‐mediated collagen binding, revealing a novel type of collagen‐binding mechanism.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.2000.01992.x</identifier><identifier>PMID: 10931316</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Adhesins, Bacterial - chemistry ; Adhesins, Bacterial - genetics ; Adhesins, Bacterial - immunology ; Adhesins, Bacterial - metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Antigens, Bacterial - immunology ; Collagen - metabolism ; Electrophoresis, Polyacrylamide Gel ; Epitope Mapping ; Humans ; Immunoblotting ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptides - chemical synthesis ; Peptides - chemistry ; Peptides - immunology ; Structure-Activity Relationship ; YadA protein ; Yersinia enterocolitica ; Yersinia enterocolitica - genetics ; Yersinia enterocolitica - metabolism ; Yersinia Infections - microbiology</subject><ispartof>Molecular microbiology, 2000-07, Vol.37 (1), p.192-206</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5012-83f97ef6256a4eccaf5e9e0554931a972142d4e137479a103a87289e042a75603</citedby><cites>FETCH-LOGICAL-c5012-83f97ef6256a4eccaf5e9e0554931a972142d4e137479a103a87289e042a75603</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-2958.2000.01992.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-2958.2000.01992.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27923,27924,45573,45574,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10931316$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tahir, Yasmin El</creatorcontrib><creatorcontrib>Kuusela, Pentti</creatorcontrib><creatorcontrib>Skurnik, Mikael</creatorcontrib><title>Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>The virulence plasmid‐encoded YadA of Yersinia enterocolitica serotype O:3 is a 430‐amino‐acid outer membrane protein, synthesized with a 25‐amino‐acid signal peptide. YadA forms homotrimeric surface structures that function as adhesin between bacteria and collagen as well as other host proteins. The structure–function relationships of YadA were studied, and the collagen‐binding determinants of YadA were located to its amino‐terminal half. Collagen did not bind to any of the overlapping 16‐mer YadA peptides, indicating that the collagen binding site of YadA is conformational. Epitope mapping of YadA identified 12 linear antigenic epitopes altogether. Seven epitopes were uniquely recognized by an anti‐YadA antiserum able to inhibit collagen binding. Four of these epitopes shared a motif NSVAIG–S that is repeated eight times within the N‐terminal half of YadA. Site‐directed mutagenesis showed that these motifs are absolutely required for YadA‐mediated collagen binding, revealing a novel type of collagen‐binding mechanism.</description><subject>Adhesins, Bacterial - chemistry</subject><subject>Adhesins, Bacterial - genetics</subject><subject>Adhesins, Bacterial - immunology</subject><subject>Adhesins, Bacterial - metabolism</subject><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>Antigens, Bacterial - immunology</subject><subject>Collagen - metabolism</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Epitope Mapping</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Peptides - immunology</subject><subject>Structure-Activity Relationship</subject><subject>YadA protein</subject><subject>Yersinia enterocolitica</subject><subject>Yersinia enterocolitica - genetics</subject><subject>Yersinia enterocolitica - metabolism</subject><subject>Yersinia Infections - microbiology</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUctu1DAUtRAVHQq_gLxil-BH7CQLFqOKlpH6WLQgurLc5GbGo8Qe4kxpd_0EJH6FL-qXcN0pFUtWvtJ5WocQylnOWaE_rHMutcpErapcMMZyxuta5LcvyOwZeElmrFYsk5X4tk9ex7hmjEum5Suyz1ktueR6Rn4fbX0zueBtTwe72Ti_pKGj0wroFYzReWcp-AnG0ITeTa6x1LYrQIBe2Xae00WLsOsQSC5JC265mujZxdf54pg-3P-iF3QISIkURcnYDs6Hh_uf6IoXBq9s3_1N3YxhAiQ6fxP6G2iTCKN7uwRPr51vseEbstfZPsLbp_eAfDn6dHn4OTs5P14czk-yRjEuskp2dQmdFkrbAprGdgpqYEoV-Htbl4IXoi2Ay7Ioa8uZtFUpKmQUwpZKM3lA3u98sdT3LcTJDC42gGU8hG00vKyE1gVHYrUjNmOIcYTObEY32PHOcGbSYmZt0jAmDWPSYuZxMXOL0ndPGdvrAdp_hLuJkPBxR_jherj7b2NzerpIl_wDpCmoOw</recordid><startdate>200007</startdate><enddate>200007</enddate><creator>Tahir, Yasmin El</creator><creator>Kuusela, Pentti</creator><creator>Skurnik, Mikael</creator><general>Blackwell Science Ltd</general><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>C1K</scope></search><sort><creationdate>200007</creationdate><title>Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding</title><author>Tahir, Yasmin El ; Kuusela, Pentti ; Skurnik, Mikael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5012-83f97ef6256a4eccaf5e9e0554931a972142d4e137479a103a87289e042a75603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adhesins, Bacterial - chemistry</topic><topic>Adhesins, Bacterial - genetics</topic><topic>Adhesins, Bacterial - immunology</topic><topic>Adhesins, Bacterial - metabolism</topic><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>Antigens, Bacterial - immunology</topic><topic>Collagen - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Epitope Mapping</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Peptides - immunology</topic><topic>Structure-Activity Relationship</topic><topic>YadA protein</topic><topic>Yersinia enterocolitica</topic><topic>Yersinia enterocolitica - genetics</topic><topic>Yersinia enterocolitica - metabolism</topic><topic>Yersinia Infections - microbiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tahir, Yasmin El</creatorcontrib><creatorcontrib>Kuusela, Pentti</creatorcontrib><creatorcontrib>Skurnik, Mikael</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tahir, Yasmin El</au><au>Kuusela, Pentti</au><au>Skurnik, Mikael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2000-07</date><risdate>2000</risdate><volume>37</volume><issue>1</issue><spage>192</spage><epage>206</epage><pages>192-206</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>The virulence plasmid‐encoded YadA of Yersinia enterocolitica serotype O:3 is a 430‐amino‐acid outer membrane protein, synthesized with a 25‐amino‐acid signal peptide. YadA forms homotrimeric surface structures that function as adhesin between bacteria and collagen as well as other host proteins. The structure–function relationships of YadA were studied, and the collagen‐binding determinants of YadA were located to its amino‐terminal half. Collagen did not bind to any of the overlapping 16‐mer YadA peptides, indicating that the collagen binding site of YadA is conformational. Epitope mapping of YadA identified 12 linear antigenic epitopes altogether. Seven epitopes were uniquely recognized by an anti‐YadA antiserum able to inhibit collagen binding. Four of these epitopes shared a motif NSVAIG–S that is repeated eight times within the N‐terminal half of YadA. Site‐directed mutagenesis showed that these motifs are absolutely required for YadA‐mediated collagen binding, revealing a novel type of collagen‐binding mechanism.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>10931316</pmid><doi>10.1046/j.1365-2958.2000.01992.x</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0950-382X |
| ispartof | Molecular microbiology, 2000-07, Vol.37 (1), p.192-206 |
| issn | 0950-382X 1365-2958 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_17826641 |
| source | MEDLINE; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; Free Full-Text Journals in Chemistry |
| subjects | Adhesins, Bacterial - chemistry Adhesins, Bacterial - genetics Adhesins, Bacterial - immunology Adhesins, Bacterial - metabolism Amino Acid Motifs Amino Acid Sequence Antigens, Bacterial - immunology Collagen - metabolism Electrophoresis, Polyacrylamide Gel Epitope Mapping Humans Immunoblotting Molecular Sequence Data Mutagenesis, Site-Directed Peptides - chemical synthesis Peptides - chemistry Peptides - immunology Structure-Activity Relationship YadA protein Yersinia enterocolitica Yersinia enterocolitica - genetics Yersinia enterocolitica - metabolism Yersinia Infections - microbiology |
| title | Functional mapping of the Yersinia enterocolitica adhesin YadA. Identification of eight NSVAIG – S motifs in the amino‐terminal half of the protein involved in collagen binding |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T02%3A20%3A14IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20mapping%20of%20the%20Yersinia%20enterocolitica%20adhesin%20YadA.%20Identification%20of%20eight%20NSVAIG%20%E2%80%93%20S%20motifs%20in%20the%20amino%E2%80%90terminal%20half%20of%20the%20protein%20involved%20in%20collagen%20binding&rft.jtitle=Molecular%20microbiology&rft.au=Tahir,%20Yasmin%20El&rft.date=2000-07&rft.volume=37&rft.issue=1&rft.spage=192&rft.epage=206&rft.pages=192-206&rft.issn=0950-382X&rft.eissn=1365-2958&rft_id=info:doi/10.1046/j.1365-2958.2000.01992.x&rft_dat=%3Cproquest_cross%3E17826641%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=17826641&rft_id=info:pmid/10931316&rfr_iscdi=true |