Inter-kingdom Signaling by the Legionella Quorum Sensing Molecule LAI-1 Modulates Cell Migration through an IQGAP1-Cdc42-ARHGEF9-Dependent Pathway
Small molecule signaling promotes the communication between bacteria as well as between bacteria and eukaryotes. The opportunistic pathogenic bacterium Legionella pneumophila employs LAI-1 (3-hydroxypentadecane-4-one) for bacterial cell-cell communication. LAI-1 is produced and detected by the Lqs (...
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| description | Small molecule signaling promotes the communication between bacteria as well as between bacteria and eukaryotes. The opportunistic pathogenic bacterium Legionella pneumophila employs LAI-1 (3-hydroxypentadecane-4-one) for bacterial cell-cell communication. LAI-1 is produced and detected by the Lqs (Legionella quorum sensing) system, which regulates a variety of processes including natural competence for DNA uptake and pathogen-host cell interactions. In this study, we analyze the role of LAI-1 in inter-kingdom signaling. L. pneumophila lacking the autoinducer synthase LqsA no longer impeded the migration of infected cells, and the defect was complemented by plasmid-borne lqsA. Synthetic LAI-1 dose-dependently inhibited cell migration, without affecting bacterial uptake or cytotoxicity. The forward migration index but not the velocity of LAI-1-treated cells was reduced, and the cell cytoskeleton appeared destabilized. LAI-1-dependent inhibition of cell migration involved the scaffold protein IQGAP1, the small GTPase Cdc42 as well as the Cdc42-specific guanine nucleotide exchange factor ARHGEF9, but not other modulators of Cdc42, or RhoA, Rac1 or Ran GTPase. Upon treatment with LAI-1, Cdc42 was inactivated and IQGAP1 redistributed to the cell cortex regardless of whether Cdc42 was present or not. Furthermore, LAI-1 reversed the inhibition of cell migration by L. pneumophila, suggesting that the compound and the bacteria antagonistically target host signaling pathway(s). Collectively, the results indicate that the L. pneumophila quorum sensing compound LAI-1 modulates migration of eukaryotic cells through a signaling pathway involving IQGAP1, Cdc42 and ARHGEF9. |
| doi_str_mv | 10.1371/journal.ppat.1005307 |
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The opportunistic pathogenic bacterium Legionella pneumophila employs LAI-1 (3-hydroxypentadecane-4-one) for bacterial cell-cell communication. LAI-1 is produced and detected by the Lqs (Legionella quorum sensing) system, which regulates a variety of processes including natural competence for DNA uptake and pathogen-host cell interactions. In this study, we analyze the role of LAI-1 in inter-kingdom signaling. L. pneumophila lacking the autoinducer synthase LqsA no longer impeded the migration of infected cells, and the defect was complemented by plasmid-borne lqsA. Synthetic LAI-1 dose-dependently inhibited cell migration, without affecting bacterial uptake or cytotoxicity. The forward migration index but not the velocity of LAI-1-treated cells was reduced, and the cell cytoskeleton appeared destabilized. LAI-1-dependent inhibition of cell migration involved the scaffold protein IQGAP1, the small GTPase Cdc42 as well as the Cdc42-specific guanine nucleotide exchange factor ARHGEF9, but not other modulators of Cdc42, or RhoA, Rac1 or Ran GTPase. Upon treatment with LAI-1, Cdc42 was inactivated and IQGAP1 redistributed to the cell cortex regardless of whether Cdc42 was present or not. Furthermore, LAI-1 reversed the inhibition of cell migration by L. pneumophila, suggesting that the compound and the bacteria antagonistically target host signaling pathway(s). Collectively, the results indicate that the L. pneumophila quorum sensing compound LAI-1 modulates migration of eukaryotic cells through a signaling pathway involving IQGAP1, Cdc42 and ARHGEF9.</description><identifier>ISSN: 1553-7374</identifier><identifier>ISSN: 1553-7366</identifier><identifier>EISSN: 1553-7374</identifier><identifier>DOI: 10.1371/journal.ppat.1005307</identifier><identifier>PMID: 26633832</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>4-Butyrolactone - analogs & derivatives ; 4-Butyrolactone - metabolism ; Animals ; Bacteria ; Bacterial Proteins - metabolism ; Bacteriology ; Blotting, Western ; cdc42 GTP-Binding Protein - metabolism ; Cell adhesion & migration ; Cell Line ; Cell migration ; Cell Movement - physiology ; Communication ; Experiments ; Gene expression ; Host-Parasite Interactions - physiology ; Kinases ; Legionella ; Legionella pneumophila ; Legionnaires disease ; Legionnaires' Disease - metabolism ; Localization ; Microbial Interactions ; Microbiological research ; Microscopy, Fluorescence ; Molecular weight ; Motility ; Phosphorylation ; Quorum Sensing - physiology ; ras GTPase-Activating Proteins - metabolism ; Real-Time Polymerase Chain Reaction ; Rho Guanine Nucleotide Exchange Factors - metabolism ; RNA, Small Interfering ; Signal Transduction - physiology ; Transfection</subject><ispartof>PLoS pathogens, 2015-12, Vol.11 (12), p.e1005307-e1005307</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Simon et al 2015 Simon et al</rights><rights>2015 Public Library of Science. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited: Quorum Sensing Molecule LAI-1 Modulates Cell Migration through an IQGAP1-Cdc42-ARHGEF9-Dependent Pathway. 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The opportunistic pathogenic bacterium Legionella pneumophila employs LAI-1 (3-hydroxypentadecane-4-one) for bacterial cell-cell communication. LAI-1 is produced and detected by the Lqs (Legionella quorum sensing) system, which regulates a variety of processes including natural competence for DNA uptake and pathogen-host cell interactions. In this study, we analyze the role of LAI-1 in inter-kingdom signaling. L. pneumophila lacking the autoinducer synthase LqsA no longer impeded the migration of infected cells, and the defect was complemented by plasmid-borne lqsA. Synthetic LAI-1 dose-dependently inhibited cell migration, without affecting bacterial uptake or cytotoxicity. The forward migration index but not the velocity of LAI-1-treated cells was reduced, and the cell cytoskeleton appeared destabilized. LAI-1-dependent inhibition of cell migration involved the scaffold protein IQGAP1, the small GTPase Cdc42 as well as the Cdc42-specific guanine nucleotide exchange factor ARHGEF9, but not other modulators of Cdc42, or RhoA, Rac1 or Ran GTPase. Upon treatment with LAI-1, Cdc42 was inactivated and IQGAP1 redistributed to the cell cortex regardless of whether Cdc42 was present or not. Furthermore, LAI-1 reversed the inhibition of cell migration by L. pneumophila, suggesting that the compound and the bacteria antagonistically target host signaling pathway(s). Collectively, the results indicate that the L. pneumophila quorum sensing compound LAI-1 modulates migration of eukaryotic cells through a signaling pathway involving IQGAP1, Cdc42 and ARHGEF9.</description><subject>4-Butyrolactone - analogs & derivatives</subject><subject>4-Butyrolactone - metabolism</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Blotting, Western</subject><subject>cdc42 GTP-Binding Protein - metabolism</subject><subject>Cell adhesion & migration</subject><subject>Cell Line</subject><subject>Cell migration</subject><subject>Cell Movement - physiology</subject><subject>Communication</subject><subject>Experiments</subject><subject>Gene expression</subject><subject>Host-Parasite Interactions - physiology</subject><subject>Kinases</subject><subject>Legionella</subject><subject>Legionella pneumophila</subject><subject>Legionnaires disease</subject><subject>Legionnaires' Disease - metabolism</subject><subject>Localization</subject><subject>Microbial Interactions</subject><subject>Microbiological research</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular weight</subject><subject>Motility</subject><subject>Phosphorylation</subject><subject>Quorum Sensing - physiology</subject><subject>ras GTPase-Activating Proteins - metabolism</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Rho Guanine Nucleotide Exchange Factors - metabolism</subject><subject>RNA, Small Interfering</subject><subject>Signal Transduction - physiology</subject><subject>Transfection</subject><issn>1553-7374</issn><issn>1553-7366</issn><issn>1553-7374</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>D8T</sourceid><sourceid>DOA</sourceid><recordid>eNqVk11v0zAUhiMEYqPwDxBE4gYuUuz4K7lBirqtq9TBPoBby7Hd1CWNix0z-jf4xThrN60SN8gX9rGf97V97JMkryEYQ8Tgx5UNrhPteLMR_RgCQBBgT5JjSAjKGGL46aPxUfLC-xUAGCJInydHOaUIFSg_Tv7Mul677IfpGmXX6Y1pomcM0nqb9kudznVjbKfbVqRXwboQEd35AbiwrZahjUg1y2AMVWhFr306iXR6YRon-iiNLs6GZpmKLp1dTatLmE2UxHlWXZ9PT8_K7ERvdKd016eXol_eiu3L5NlCtF6_2vej5NvZ6dfJeTb_Mp1NqnkmKYN9RgqMSVljghaSMVlDqhYUS0EhIASSGsCyrkWONVFIlwQwWrMa5DgHqGRMYTRK3u58N631fJ9OzyFjqKAI5kUkZjtCWbHiG2fWwm25FYbfTVjXcOF6I1vNSUFLUSNGpNAYK1xAReOOmAClaV3C6JXtvPyt3oT6wO3EfK_u3MI6cAgxQnnkP-1PF-q1VjImyIn2QHa40pklb-wvjiktIRwO_35v4OzPoH3P18bL4SU7bcNwTxzRPI8fZ5S826GNiFcx3cJGRzngvMIE42LAIjX-BxWb0msj4ydZmDh_IPhwIIhMr3_3jQje89nN9X-wnw9ZvGOls947vXjICgR8qI37x-RDbfB9bUTZm8cZfRDdFwP6C8M7CL0</recordid><startdate>20151201</startdate><enddate>20151201</enddate><creator>Simon, Sylvia</creator><creator>Schell, Ursula</creator><creator>Heuer, Natalie</creator><creator>Hager, Dominik</creator><creator>Albers, Michael F</creator><creator>Matthias, Jan</creator><creator>Fahrnbauer, Felix</creator><creator>Trauner, Dirk</creator><creator>Eichinger, Ludwig</creator><creator>Hedberg, Christian</creator><creator>Hilbi, Hubert</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>ISN</scope><scope>ISR</scope><scope>7X8</scope><scope>5PM</scope><scope>ADHXS</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>D93</scope><scope>ZZAVC</scope><scope>DOA</scope></search><sort><creationdate>20151201</creationdate><title>Inter-kingdom Signaling by the Legionella Quorum Sensing Molecule LAI-1 Modulates Cell Migration through an IQGAP1-Cdc42-ARHGEF9-Dependent Pathway</title><author>Simon, Sylvia ; Schell, Ursula ; Heuer, Natalie ; Hager, Dominik ; Albers, Michael F ; Matthias, Jan ; Fahrnbauer, Felix ; Trauner, Dirk ; Eichinger, Ludwig ; Hedberg, Christian ; Hilbi, Hubert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c671t-584459b453fc77cb16df64ca6105515b019bba24e5d3e95076b7b024203977d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>4-Butyrolactone - analogs & derivatives</topic><topic>4-Butyrolactone - metabolism</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Blotting, Western</topic><topic>cdc42 GTP-Binding Protein - metabolism</topic><topic>Cell adhesion & migration</topic><topic>Cell Line</topic><topic>Cell migration</topic><topic>Cell Movement - physiology</topic><topic>Communication</topic><topic>Experiments</topic><topic>Gene expression</topic><topic>Host-Parasite Interactions - physiology</topic><topic>Kinases</topic><topic>Legionella</topic><topic>Legionella pneumophila</topic><topic>Legionnaires disease</topic><topic>Legionnaires' Disease - metabolism</topic><topic>Localization</topic><topic>Microbial Interactions</topic><topic>Microbiological research</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular weight</topic><topic>Motility</topic><topic>Phosphorylation</topic><topic>Quorum Sensing - physiology</topic><topic>ras GTPase-Activating Proteins - metabolism</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Rho Guanine Nucleotide Exchange Factors - metabolism</topic><topic>RNA, Small Interfering</topic><topic>Signal Transduction - physiology</topic><topic>Transfection</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Simon, Sylvia</creatorcontrib><creatorcontrib>Schell, Ursula</creatorcontrib><creatorcontrib>Heuer, Natalie</creatorcontrib><creatorcontrib>Hager, Dominik</creatorcontrib><creatorcontrib>Albers, Michael F</creatorcontrib><creatorcontrib>Matthias, Jan</creatorcontrib><creatorcontrib>Fahrnbauer, Felix</creatorcontrib><creatorcontrib>Trauner, Dirk</creatorcontrib><creatorcontrib>Eichinger, Ludwig</creatorcontrib><creatorcontrib>Hedberg, Christian</creatorcontrib><creatorcontrib>Hilbi, Hubert</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Canada</collection><collection>Gale In Context: Science</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SWEPUB Umeå universitet full text</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SWEPUB Umeå universitet</collection><collection>SwePub Articles full text</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PLoS pathogens</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Simon, Sylvia</au><au>Schell, Ursula</au><au>Heuer, Natalie</au><au>Hager, Dominik</au><au>Albers, Michael F</au><au>Matthias, Jan</au><au>Fahrnbauer, Felix</au><au>Trauner, Dirk</au><au>Eichinger, Ludwig</au><au>Hedberg, Christian</au><au>Hilbi, Hubert</au><au>Kubori, Tomoko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inter-kingdom Signaling by the Legionella Quorum Sensing Molecule LAI-1 Modulates Cell Migration through an IQGAP1-Cdc42-ARHGEF9-Dependent Pathway</atitle><jtitle>PLoS pathogens</jtitle><addtitle>PLoS Pathog</addtitle><date>2015-12-01</date><risdate>2015</risdate><volume>11</volume><issue>12</issue><spage>e1005307</spage><epage>e1005307</epage><pages>e1005307-e1005307</pages><issn>1553-7374</issn><issn>1553-7366</issn><eissn>1553-7374</eissn><abstract>Small molecule signaling promotes the communication between bacteria as well as between bacteria and eukaryotes. The opportunistic pathogenic bacterium Legionella pneumophila employs LAI-1 (3-hydroxypentadecane-4-one) for bacterial cell-cell communication. LAI-1 is produced and detected by the Lqs (Legionella quorum sensing) system, which regulates a variety of processes including natural competence for DNA uptake and pathogen-host cell interactions. In this study, we analyze the role of LAI-1 in inter-kingdom signaling. L. pneumophila lacking the autoinducer synthase LqsA no longer impeded the migration of infected cells, and the defect was complemented by plasmid-borne lqsA. Synthetic LAI-1 dose-dependently inhibited cell migration, without affecting bacterial uptake or cytotoxicity. The forward migration index but not the velocity of LAI-1-treated cells was reduced, and the cell cytoskeleton appeared destabilized. LAI-1-dependent inhibition of cell migration involved the scaffold protein IQGAP1, the small GTPase Cdc42 as well as the Cdc42-specific guanine nucleotide exchange factor ARHGEF9, but not other modulators of Cdc42, or RhoA, Rac1 or Ran GTPase. Upon treatment with LAI-1, Cdc42 was inactivated and IQGAP1 redistributed to the cell cortex regardless of whether Cdc42 was present or not. Furthermore, LAI-1 reversed the inhibition of cell migration by L. pneumophila, suggesting that the compound and the bacteria antagonistically target host signaling pathway(s). Collectively, the results indicate that the L. pneumophila quorum sensing compound LAI-1 modulates migration of eukaryotic cells through a signaling pathway involving IQGAP1, Cdc42 and ARHGEF9.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26633832</pmid><doi>10.1371/journal.ppat.1005307</doi><oa>free_for_read</oa></addata></record> |
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| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; SWEPUB Freely available online; PubMed Central Open Access |
| subjects | 4-Butyrolactone - analogs & derivatives 4-Butyrolactone - metabolism Animals Bacteria Bacterial Proteins - metabolism Bacteriology Blotting, Western cdc42 GTP-Binding Protein - metabolism Cell adhesion & migration Cell Line Cell migration Cell Movement - physiology Communication Experiments Gene expression Host-Parasite Interactions - physiology Kinases Legionella Legionella pneumophila Legionnaires disease Legionnaires' Disease - metabolism Localization Microbial Interactions Microbiological research Microscopy, Fluorescence Molecular weight Motility Phosphorylation Quorum Sensing - physiology ras GTPase-Activating Proteins - metabolism Real-Time Polymerase Chain Reaction Rho Guanine Nucleotide Exchange Factors - metabolism RNA, Small Interfering Signal Transduction - physiology Transfection |
| title | Inter-kingdom Signaling by the Legionella Quorum Sensing Molecule LAI-1 Modulates Cell Migration through an IQGAP1-Cdc42-ARHGEF9-Dependent Pathway |
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