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Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin
Botulinum neurotoxin is produced by Clostridium botulinum and forms large protein complexes through associations with nontoxic components. We recently found that hemagglutinin (HA), one of the nontoxic components, disrupts the intercellular epithelial barrier; however, the mechanism underlying this...
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| Published in: | The Journal of cell biology 2010-05, Vol.189 (4), p.691-700 |
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| Main Authors: | , , , , , , |
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| cites | cdi_FETCH-LOGICAL-c525t-20143a6ab43965f9ac5022680d354247adfd1a0c222a0dcfaff4c50479f44b7d3 |
| container_end_page | 700 |
| container_issue | 4 |
| container_start_page | 691 |
| container_title | The Journal of cell biology |
| container_volume | 189 |
| creator | Sugawara, Yo Matsumura, Takuhiro Takegahara, Yuki Jin, Yingji Tsukasaki, Yoshikazu Takeichi, Masatoshi Fujinaga, Yukako |
| description | Botulinum neurotoxin is produced by Clostridium botulinum and forms large protein complexes through associations with nontoxic components. We recently found that hemagglutinin (HA), one of the nontoxic components, disrupts the intercellular epithelial barrier; however, the mechanism underlying this phenomenon is not known. In this study, we identified epithelial cadherin (E-cadherin) as a target molecule for HA. HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion. Although HA binds human, bovine, and mouse E-cadherin, it does not bind rat or chicken E-cadherin homologues. HA does not interact with other members of the classical cadherin family such as neural and vascular endothelial cadherin. Expression of rat E-cadherin but not mouse rescues Madin-Darby canine kidney cells from HA-induced tight junction (TJ) disruptions. These data demonstrate that botulinum HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion in a species-specific manner and that the HA-E-cadherin interaction is essential for the disruption of TJ function. |
| doi_str_mv | 10.1083/jcb.200910119 |
| format | article |
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We recently found that hemagglutinin (HA), one of the nontoxic components, disrupts the intercellular epithelial barrier; however, the mechanism underlying this phenomenon is not known. In this study, we identified epithelial cadherin (E-cadherin) as a target molecule for HA. HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion. Although HA binds human, bovine, and mouse E-cadherin, it does not bind rat or chicken E-cadherin homologues. HA does not interact with other members of the classical cadherin family such as neural and vascular endothelial cadherin. Expression of rat E-cadherin but not mouse rescues Madin-Darby canine kidney cells from HA-induced tight junction (TJ) disruptions. These data demonstrate that botulinum HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion in a species-specific manner and that the HA-E-cadherin interaction is essential for the disruption of TJ function.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.200910119</identifier><identifier>PMID: 20457762</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: The Rockefeller University Press</publisher><subject>Animals ; Antibodies ; Botulinum Toxins - metabolism ; Botulinum Toxins - pharmacology ; Botulism ; Caco 2 cells ; Cadherins ; Cadherins - chemistry ; Cadherins - metabolism ; Canines ; Cattle ; Cell adhesion ; Cell adhesion & migration ; Cell Adhesion - drug effects ; Cell Line ; Cellular biology ; Delta cells ; Dogs ; Epithelial cells ; Epithelial Cells - cytology ; Epithelial Cells - drug effects ; Epithelial Cells - metabolism ; Gram-positive bacteria ; Hemagglutinins - metabolism ; Hemagglutinins - pharmacology ; Humans ; Intercellular junctions ; L cells ; Mice ; Neurotoxicity ; Proteins ; Rats ; Toxins</subject><ispartof>The Journal of cell biology, 2010-05, Vol.189 (4), p.691-700</ispartof><rights>Copyright Rockefeller University Press May 17, 2010</rights><rights>2010 Sugawara et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-20143a6ab43965f9ac5022680d354247adfd1a0c222a0dcfaff4c50479f44b7d3</citedby><cites>FETCH-LOGICAL-c525t-20143a6ab43965f9ac5022680d354247adfd1a0c222a0dcfaff4c50479f44b7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20457762$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sugawara, Yo</creatorcontrib><creatorcontrib>Matsumura, Takuhiro</creatorcontrib><creatorcontrib>Takegahara, Yuki</creatorcontrib><creatorcontrib>Jin, Yingji</creatorcontrib><creatorcontrib>Tsukasaki, Yoshikazu</creatorcontrib><creatorcontrib>Takeichi, Masatoshi</creatorcontrib><creatorcontrib>Fujinaga, Yukako</creatorcontrib><title>Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Botulinum neurotoxin is produced by Clostridium botulinum and forms large protein complexes through associations with nontoxic components. We recently found that hemagglutinin (HA), one of the nontoxic components, disrupts the intercellular epithelial barrier; however, the mechanism underlying this phenomenon is not known. In this study, we identified epithelial cadherin (E-cadherin) as a target molecule for HA. HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion. Although HA binds human, bovine, and mouse E-cadherin, it does not bind rat or chicken E-cadherin homologues. HA does not interact with other members of the classical cadherin family such as neural and vascular endothelial cadherin. Expression of rat E-cadherin but not mouse rescues Madin-Darby canine kidney cells from HA-induced tight junction (TJ) disruptions. These data demonstrate that botulinum HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion in a species-specific manner and that the HA-E-cadherin interaction is essential for the disruption of TJ function.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Botulinum Toxins - metabolism</subject><subject>Botulinum Toxins - pharmacology</subject><subject>Botulism</subject><subject>Caco 2 cells</subject><subject>Cadherins</subject><subject>Cadherins - chemistry</subject><subject>Cadherins - metabolism</subject><subject>Canines</subject><subject>Cattle</subject><subject>Cell adhesion</subject><subject>Cell adhesion & migration</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Line</subject><subject>Cellular biology</subject><subject>Delta cells</subject><subject>Dogs</subject><subject>Epithelial cells</subject><subject>Epithelial Cells - cytology</subject><subject>Epithelial Cells - drug effects</subject><subject>Epithelial Cells - metabolism</subject><subject>Gram-positive bacteria</subject><subject>Hemagglutinins - metabolism</subject><subject>Hemagglutinins - pharmacology</subject><subject>Humans</subject><subject>Intercellular junctions</subject><subject>L cells</subject><subject>Mice</subject><subject>Neurotoxicity</subject><subject>Proteins</subject><subject>Rats</subject><subject>Toxins</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNpVkUtv1DAUhS1ERYfCkiVgsU-5fmSSbJBKVWilSl1A19aNHxmPPM5gO0jz7zGaMoA3V_L57vGRDyFvGFwy6MXHrR4vOcDAgLHhGVmxVkLTMwnPyQqAs2ZoeXtOXua8BQDZSfGCnHOQbdet-YqYz3NZgo_Ljm7sDqcpLMVHH6nxOS37kmnZWOpjsUnbEJaAidq9r5fBY6AjpuRtouOhLiSrSzjQ0Ufj40RvGo1mY5OPr8iZw5Dt66d5QR6_3Hy_vm3uH77eXV_dN7pmLA0HJgWucZRiWLduQN0C5-sejGgllx0aZxiC5pwjGO3QOVkR2Q1OyrEz4oJ8Ovrul3FnjbaxJAxqn_wO00HN6NX_SvQbNc0_Fe87PoCsBh-eDNL8Y7G5qO28pFgzK846xsQgWIWaI6TTnHOy7vQAA_W7E1U7UadOKv_u31Qn-k8JFXh7BLa5zOmv3vWsOkDV3x91h7PCKfmsHr_VzxLAellPK34BUhicyg</recordid><startdate>20100517</startdate><enddate>20100517</enddate><creator>Sugawara, Yo</creator><creator>Matsumura, Takuhiro</creator><creator>Takegahara, Yuki</creator><creator>Jin, Yingji</creator><creator>Tsukasaki, Yoshikazu</creator><creator>Takeichi, Masatoshi</creator><creator>Fujinaga, Yukako</creator><general>The Rockefeller University Press</general><general>Rockefeller University Press</general><scope>FBQ</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><scope>5PM</scope></search><sort><creationdate>20100517</creationdate><title>Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin</title><author>Sugawara, Yo ; Matsumura, Takuhiro ; Takegahara, Yuki ; Jin, Yingji ; Tsukasaki, Yoshikazu ; Takeichi, Masatoshi ; Fujinaga, Yukako</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-20143a6ab43965f9ac5022680d354247adfd1a0c222a0dcfaff4c50479f44b7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Botulinum Toxins - metabolism</topic><topic>Botulinum Toxins - pharmacology</topic><topic>Botulism</topic><topic>Caco 2 cells</topic><topic>Cadherins</topic><topic>Cadherins - chemistry</topic><topic>Cadherins - metabolism</topic><topic>Canines</topic><topic>Cattle</topic><topic>Cell adhesion</topic><topic>Cell adhesion & migration</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Line</topic><topic>Cellular biology</topic><topic>Delta cells</topic><topic>Dogs</topic><topic>Epithelial cells</topic><topic>Epithelial Cells - cytology</topic><topic>Epithelial Cells - drug effects</topic><topic>Epithelial Cells - metabolism</topic><topic>Gram-positive bacteria</topic><topic>Hemagglutinins - metabolism</topic><topic>Hemagglutinins - pharmacology</topic><topic>Humans</topic><topic>Intercellular junctions</topic><topic>L cells</topic><topic>Mice</topic><topic>Neurotoxicity</topic><topic>Proteins</topic><topic>Rats</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sugawara, Yo</creatorcontrib><creatorcontrib>Matsumura, Takuhiro</creatorcontrib><creatorcontrib>Takegahara, Yuki</creatorcontrib><creatorcontrib>Jin, Yingji</creatorcontrib><creatorcontrib>Tsukasaki, Yoshikazu</creatorcontrib><creatorcontrib>Takeichi, Masatoshi</creatorcontrib><creatorcontrib>Fujinaga, Yukako</creatorcontrib><collection>AGRIS</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sugawara, Yo</au><au>Matsumura, Takuhiro</au><au>Takegahara, Yuki</au><au>Jin, Yingji</au><au>Tsukasaki, Yoshikazu</au><au>Takeichi, Masatoshi</au><au>Fujinaga, Yukako</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2010-05-17</date><risdate>2010</risdate><volume>189</volume><issue>4</issue><spage>691</spage><epage>700</epage><pages>691-700</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Botulinum neurotoxin is produced by Clostridium botulinum and forms large protein complexes through associations with nontoxic components. We recently found that hemagglutinin (HA), one of the nontoxic components, disrupts the intercellular epithelial barrier; however, the mechanism underlying this phenomenon is not known. In this study, we identified epithelial cadherin (E-cadherin) as a target molecule for HA. HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion. Although HA binds human, bovine, and mouse E-cadherin, it does not bind rat or chicken E-cadherin homologues. HA does not interact with other members of the classical cadherin family such as neural and vascular endothelial cadherin. Expression of rat E-cadherin but not mouse rescues Madin-Darby canine kidney cells from HA-induced tight junction (TJ) disruptions. These data demonstrate that botulinum HA directly binds E-cadherin and disrupts E-cadherin-mediated cell to cell adhesion in a species-specific manner and that the HA-E-cadherin interaction is essential for the disruption of TJ function.</abstract><cop>United States</cop><pub>The Rockefeller University Press</pub><pmid>20457762</pmid><doi>10.1083/jcb.200910119</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 2010-05, Vol.189 (4), p.691-700 |
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| source | Alma/SFX Local Collection |
| subjects | Animals Antibodies Botulinum Toxins - metabolism Botulinum Toxins - pharmacology Botulism Caco 2 cells Cadherins Cadherins - chemistry Cadherins - metabolism Canines Cattle Cell adhesion Cell adhesion & migration Cell Adhesion - drug effects Cell Line Cellular biology Delta cells Dogs Epithelial cells Epithelial Cells - cytology Epithelial Cells - drug effects Epithelial Cells - metabolism Gram-positive bacteria Hemagglutinins - metabolism Hemagglutinins - pharmacology Humans Intercellular junctions L cells Mice Neurotoxicity Proteins Rats Toxins |
| title | Botulinum hemagglutinin disrupts the intercellular epithelial barrier by directly binding E-cadherin |
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