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The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity
Summary Legionella pneumophila establishes a replication vacuole within phagocytes that requires the bacterial Dot/Icm apparatus for its formation. This apparatus is predicted to translocate effectors into host cells. We hypothesized that some translocated proteins also function to maintain the inte...
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Published in: | Molecular microbiology 2003-04, Vol.48 (2), p.305-321 |
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container_title | Molecular microbiology |
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creator | Conover, Gloria M. Derré, Isabelle Vogel, Joseph P. Isberg, Ralph R. |
description | Summary
Legionella pneumophila
establishes a replication vacuole within phagocytes that requires the bacterial Dot/Icm apparatus for its formation. This apparatus is predicted to translocate effectors into host cells. We hypothesized that some translocated proteins also function to maintain the integrity of the Dot/Icm translocator. Mutations that destroy this function are predicted to result in a Dot/Icm complex that poisons the bacterium, resulting in reduced viability. To identify such mutants, strains were isolated (called
lid
–
) that showed reduced viability on bacteriological medium in the presence of an intact Dot/Icm apparatus, but which had high viability in the absence of the translocator. Several such mutants were analysed in detail to identify candidate strains that may have lost the ability to synthesize a translocated substrate of Dot/Icm. Two such strains had mutations in the
lidA
gene. The LidA protein exhibits properties expected for a translocated substrate of Dot/Icm that is important for maintenance of bacterial cell integrity: it associates with the phagosomal surface, promotes replication vacuole formation, and is important for both efficient intracellular growth and high viability on bacteriological media after introduction of a plasmid that allows high level expression of the
dotA gene. |
doi_str_mv | 10.1046/j.1365-2958.2003.03400.x |
format | article |
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Legionella pneumophila
establishes a replication vacuole within phagocytes that requires the bacterial Dot/Icm apparatus for its formation. This apparatus is predicted to translocate effectors into host cells. We hypothesized that some translocated proteins also function to maintain the integrity of the Dot/Icm translocator. Mutations that destroy this function are predicted to result in a Dot/Icm complex that poisons the bacterium, resulting in reduced viability. To identify such mutants, strains were isolated (called
lid
–
) that showed reduced viability on bacteriological medium in the presence of an intact Dot/Icm apparatus, but which had high viability in the absence of the translocator. Several such mutants were analysed in detail to identify candidate strains that may have lost the ability to synthesize a translocated substrate of Dot/Icm. Two such strains had mutations in the
lidA
gene. The LidA protein exhibits properties expected for a translocated substrate of Dot/Icm that is important for maintenance of bacterial cell integrity: it associates with the phagosomal surface, promotes replication vacuole formation, and is important for both efficient intracellular growth and high viability on bacteriological media after introduction of a plasmid that allows high level expression of the
dotA gene.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1046/j.1365-2958.2003.03400.x</identifier><identifier>PMID: 12675793</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Animals ; Antigens, CD - metabolism ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bone Marrow Cells - cytology ; Bone Marrow Cells - metabolism ; Bone Marrow Cells - microbiology ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Cells, Cultured ; Female ; Humans ; Legionella pneumophila - genetics ; Legionella pneumophila - metabolism ; Lysosomal Membrane Proteins ; Macrophages - cytology ; Macrophages - metabolism ; Macrophages - microbiology ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane Transport Proteins - metabolism ; Mice ; Mutation ; Phagosomes - metabolism</subject><ispartof>Molecular microbiology, 2003-04, Vol.48 (2), p.305-321</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3780-320404c48420f3acc820e4b36290db57126f013fce0b36b5dcbd114b4c15d2b73</citedby><cites>FETCH-LOGICAL-c3780-320404c48420f3acc820e4b36290db57126f013fce0b36b5dcbd114b4c15d2b73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12675793$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Conover, Gloria M.</creatorcontrib><creatorcontrib>Derré, Isabelle</creatorcontrib><creatorcontrib>Vogel, Joseph P.</creatorcontrib><creatorcontrib>Isberg, Ralph R.</creatorcontrib><title>The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Summary
Legionella pneumophila
establishes a replication vacuole within phagocytes that requires the bacterial Dot/Icm apparatus for its formation. This apparatus is predicted to translocate effectors into host cells. We hypothesized that some translocated proteins also function to maintain the integrity of the Dot/Icm translocator. Mutations that destroy this function are predicted to result in a Dot/Icm complex that poisons the bacterium, resulting in reduced viability. To identify such mutants, strains were isolated (called
lid
–
) that showed reduced viability on bacteriological medium in the presence of an intact Dot/Icm apparatus, but which had high viability in the absence of the translocator. Several such mutants were analysed in detail to identify candidate strains that may have lost the ability to synthesize a translocated substrate of Dot/Icm. Two such strains had mutations in the
lidA
gene. The LidA protein exhibits properties expected for a translocated substrate of Dot/Icm that is important for maintenance of bacterial cell integrity: it associates with the phagosomal surface, promotes replication vacuole formation, and is important for both efficient intracellular growth and high viability on bacteriological media after introduction of a plasmid that allows high level expression of the
dotA gene.</description><subject>Animals</subject><subject>Antigens, CD - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bone Marrow Cells - cytology</subject><subject>Bone Marrow Cells - metabolism</subject><subject>Bone Marrow Cells - microbiology</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Cells, Cultured</subject><subject>Female</subject><subject>Humans</subject><subject>Legionella pneumophila - genetics</subject><subject>Legionella pneumophila - metabolism</subject><subject>Lysosomal Membrane Proteins</subject><subject>Macrophages - cytology</subject><subject>Macrophages - metabolism</subject><subject>Macrophages - microbiology</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Transport Proteins - metabolism</subject><subject>Mice</subject><subject>Mutation</subject><subject>Phagosomes - metabolism</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqNUctu2zAQJIoGjZv2FwqeerOyfOhVoIcgaRsDDnJJgNwIklrFNCTRFSkk_oV-dSnbSK89cbGcmcXMEEIZZAxkcbnNmCjyJa_zKuMAIgMhAbLXd2Tx9vGeLKDOYSkq_nROPoawBWACCvGBnDNelHlZiwX587BBusZn5wfsOk13A069321cmteuuaK70Ud0wzeqaRz1EDpvdcSGhsmEtIhIfUtjErnx8XJlexr2IWJPdQjeugP0xcUN7bUbIg56sAeG0Tbi6HRH5_Xz6OL-EzlrdRfw8-m9II8_fzxc3y7X979W11frpRVllfxwkCCtrCSHVmhrKw4ojSh4DY3Jy-StTUZbi5CWJm-saRiTRlqWN9yU4oJ8Peoma78nDFH1LtjZ_YB-CopVJSvqiiVgdQTa0YcwYqt2o-v1uFcM1NyD2qo5bjXHreYe1KEH9ZqoX043JtNj8494Cj4Bvh8BL67D_X8Lq7u71TyJv7-7mOU</recordid><startdate>200304</startdate><enddate>200304</enddate><creator>Conover, Gloria M.</creator><creator>Derré, Isabelle</creator><creator>Vogel, Joseph P.</creator><creator>Isberg, Ralph R.</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>200304</creationdate><title>The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity</title><author>Conover, Gloria M. ; Derré, Isabelle ; Vogel, Joseph P. ; Isberg, Ralph R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3780-320404c48420f3acc820e4b36290db57126f013fce0b36b5dcbd114b4c15d2b73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Antigens, CD - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bone Marrow Cells - cytology</topic><topic>Bone Marrow Cells - metabolism</topic><topic>Bone Marrow Cells - microbiology</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Cells, Cultured</topic><topic>Female</topic><topic>Humans</topic><topic>Legionella pneumophila - genetics</topic><topic>Legionella pneumophila - metabolism</topic><topic>Lysosomal Membrane Proteins</topic><topic>Macrophages - cytology</topic><topic>Macrophages - metabolism</topic><topic>Macrophages - microbiology</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Transport Proteins - metabolism</topic><topic>Mice</topic><topic>Mutation</topic><topic>Phagosomes - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Conover, Gloria M.</creatorcontrib><creatorcontrib>Derré, Isabelle</creatorcontrib><creatorcontrib>Vogel, Joseph P.</creatorcontrib><creatorcontrib>Isberg, Ralph R.</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</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>Conover, Gloria M.</au><au>Derré, Isabelle</au><au>Vogel, Joseph P.</au><au>Isberg, Ralph R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2003-04</date><risdate>2003</risdate><volume>48</volume><issue>2</issue><spage>305</spage><epage>321</epage><pages>305-321</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Summary
Legionella pneumophila
establishes a replication vacuole within phagocytes that requires the bacterial Dot/Icm apparatus for its formation. This apparatus is predicted to translocate effectors into host cells. We hypothesized that some translocated proteins also function to maintain the integrity of the Dot/Icm translocator. Mutations that destroy this function are predicted to result in a Dot/Icm complex that poisons the bacterium, resulting in reduced viability. To identify such mutants, strains were isolated (called
lid
–
) that showed reduced viability on bacteriological medium in the presence of an intact Dot/Icm apparatus, but which had high viability in the absence of the translocator. Several such mutants were analysed in detail to identify candidate strains that may have lost the ability to synthesize a translocated substrate of Dot/Icm. Two such strains had mutations in the
lidA
gene. The LidA protein exhibits properties expected for a translocated substrate of Dot/Icm that is important for maintenance of bacterial cell integrity: it associates with the phagosomal surface, promotes replication vacuole formation, and is important for both efficient intracellular growth and high viability on bacteriological media after introduction of a plasmid that allows high level expression of the
dotA gene.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>12675793</pmid><doi>10.1046/j.1365-2958.2003.03400.x</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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source | Wiley-Blackwell Read & Publish Collection |
subjects | Animals Antigens, CD - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Bone Marrow Cells - cytology Bone Marrow Cells - metabolism Bone Marrow Cells - microbiology Carrier Proteins - genetics Carrier Proteins - metabolism Cell Membrane - metabolism Cells, Cultured Female Humans Legionella pneumophila - genetics Legionella pneumophila - metabolism Lysosomal Membrane Proteins Macrophages - cytology Macrophages - metabolism Macrophages - microbiology Membrane Proteins - genetics Membrane Proteins - metabolism Membrane Transport Proteins - metabolism Mice Mutation Phagosomes - metabolism |
title | The Legionella pneumophila LidA protein: a translocated substrate of the Dot/Icm system associated with maintenance of bacterial integrity |
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