Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence
Leptospira interrogans is the causative agent of leptospirosis. Lipopolysaccharide (LPS) is the major outer membrane component of L. interrogans. It is the dominant antigen recognized during infection and the basis for serological classification. The structure of LPS and its role in pathogenesis are...
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| Veröffentlicht in: | Molecular microbiology 2010-11, Vol.78 (3), p.701-709 |
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| creator | Murray, Gerald L Srikram, Amporn Henry, Rebekah Hartskeerl, Rudy A Sermswan, Rasana W Adler, Ben |
| description | Leptospira interrogans is the causative agent of leptospirosis. Lipopolysaccharide (LPS) is the major outer membrane component of L. interrogans. It is the dominant antigen recognized during infection and the basis for serological classification. The structure of LPS and its role in pathogenesis are unknown. We describe two defined mutants of L. interrogans serovar Manilae with transposon insertions in the LPS locus. Mutant M895 was disrupted in gene la1641 encoding a protein with no known homologues. M1352 was disrupted in a gene unique to serovar Manilae also encoding a protein of unknown function. M895 produced truncated LPS while M1352 showed little or no change in LPS molecular mass. Both mutants showed altered agglutination titres against rabbit antiserum and against a panel of LPS‐specific monoclonal antibodies. The mutants were severely attenuated in virulence via the intraperitoneal route of infection, and were cleared from the host animal by 3 days after infection. M895 was also highly attenuated via the mucosal infection route. Resistance to complement in human serum was unaltered for both mutants. While complementation of mutants was not possible, the attenuation of two independently derived LPS mutants demonstrates for the first time that LPS plays an essential role leptospiral virulence. |
| doi_str_mv | 10.1111/j.1365-2958.2010.07360.x |
| format | Article |
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Lipopolysaccharide (LPS) is the major outer membrane component of L. interrogans. It is the dominant antigen recognized during infection and the basis for serological classification. The structure of LPS and its role in pathogenesis are unknown. We describe two defined mutants of L. interrogans serovar Manilae with transposon insertions in the LPS locus. Mutant M895 was disrupted in gene la1641 encoding a protein with no known homologues. M1352 was disrupted in a gene unique to serovar Manilae also encoding a protein of unknown function. M895 produced truncated LPS while M1352 showed little or no change in LPS molecular mass. Both mutants showed altered agglutination titres against rabbit antiserum and against a panel of LPS‐specific monoclonal antibodies. The mutants were severely attenuated in virulence via the intraperitoneal route of infection, and were cleared from the host animal by 3 days after infection. M895 was also highly attenuated via the mucosal infection route. Resistance to complement in human serum was unaltered for both mutants. While complementation of mutants was not possible, the attenuation of two independently derived LPS mutants demonstrates for the first time that LPS plays an essential role leptospiral virulence.</description><identifier>ISSN: 0950-382X</identifier><identifier>EISSN: 1365-2958</identifier><identifier>DOI: 10.1111/j.1365-2958.2010.07360.x</identifier><identifier>PMID: 20807198</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Animals ; Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Bacteriology ; Biological and medical sciences ; Cricetinae ; Fundamental and applied biological sciences. Psychology ; Humans ; Leptospira interrogans ; Leptospira interrogans - genetics ; Leptospira interrogans - metabolism ; Leptospira interrogans - pathogenicity ; Leptospirosis - microbiology ; Lipopolysaccharides - deficiency ; Lipopolysaccharides - genetics ; Membranes ; Mesocricetus ; Microbiology ; Miscellaneous ; Molecular biology ; Mutagenesis, Insertional ; Mutation ; Pathogenesis ; Proteins ; Virulence</subject><ispartof>Molecular microbiology, 2010-11, Vol.78 (3), p.701-709</ispartof><rights>2010 Blackwell Publishing Ltd</rights><rights>2015 INIST-CNRS</rights><rights>2010 Blackwell Publishing Ltd.</rights><rights>Copyright Blackwell Publishing Ltd. Nov 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5970-96a481bed1f24069e0ffe8ac2c4914f188ce3f22cc250d2ba92c05ee181da33</citedby><cites>FETCH-LOGICAL-c5970-96a481bed1f24069e0ffe8ac2c4914f188ce3f22cc250d2ba92c05ee181da33</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.1365-2958.2010.07360.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1365-2958.2010.07360.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,1433,27923,27924,45573,45574,46408,46832</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23366612$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20807198$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murray, Gerald L</creatorcontrib><creatorcontrib>Srikram, Amporn</creatorcontrib><creatorcontrib>Henry, Rebekah</creatorcontrib><creatorcontrib>Hartskeerl, Rudy A</creatorcontrib><creatorcontrib>Sermswan, Rasana W</creatorcontrib><creatorcontrib>Adler, Ben</creatorcontrib><title>Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence</title><title>Molecular microbiology</title><addtitle>Mol Microbiol</addtitle><description>Leptospira interrogans is the causative agent of leptospirosis. Lipopolysaccharide (LPS) is the major outer membrane component of L. interrogans. It is the dominant antigen recognized during infection and the basis for serological classification. The structure of LPS and its role in pathogenesis are unknown. We describe two defined mutants of L. interrogans serovar Manilae with transposon insertions in the LPS locus. Mutant M895 was disrupted in gene la1641 encoding a protein with no known homologues. M1352 was disrupted in a gene unique to serovar Manilae also encoding a protein of unknown function. M895 produced truncated LPS while M1352 showed little or no change in LPS molecular mass. Both mutants showed altered agglutination titres against rabbit antiserum and against a panel of LPS‐specific monoclonal antibodies. The mutants were severely attenuated in virulence via the intraperitoneal route of infection, and were cleared from the host animal by 3 days after infection. M895 was also highly attenuated via the mucosal infection route. Resistance to complement in human serum was unaltered for both mutants. While complementation of mutants was not possible, the attenuation of two independently derived LPS mutants demonstrates for the first time that LPS plays an essential role leptospiral virulence.</description><subject>Animals</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Cricetinae</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Leptospira interrogans</subject><subject>Leptospira interrogans - genetics</subject><subject>Leptospira interrogans - metabolism</subject><subject>Leptospira interrogans - pathogenicity</subject><subject>Leptospirosis - microbiology</subject><subject>Lipopolysaccharides - deficiency</subject><subject>Lipopolysaccharides - genetics</subject><subject>Membranes</subject><subject>Mesocricetus</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Molecular biology</subject><subject>Mutagenesis, Insertional</subject><subject>Mutation</subject><subject>Pathogenesis</subject><subject>Proteins</subject><subject>Virulence</subject><issn>0950-382X</issn><issn>1365-2958</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkkGP1CAUx4nRuOPqV9DGxOyp4wMKhYOHzcbVTWZizGrijbyhdGTSKRVa3fn2UmdcEy_KBQK__3uQH4QUFJY0j9e7JeVSlEwLtWSQd6HmEpZ3D8ji_uAhWYAWUHLFvpyRJyntACgHyR-TMwYKaqrVgnxcTyOOPvSpwLZ1dvT9tli5YQxp8BEL348uxrDFDHR-CEPoDgmt_YrRN67AcXT9hKMrvvs4da637il51GKX3LPTfE5ur99-unpfrj68u7m6XJVW6BpKLbFSdOMa2rIKpHaQ2yu0zFaaVi1VyjreMmYtE9CwDWpmQThHFW2Q83Nycaw6xPBtcmk0e5-s6zrsXZiSUVQIritd_5OsJTAuFBeZfPkXuQtT7PMjjAJGK1ZpmSF1hGwMKUXXmiH6PcaDoWBmOWZnZgdmdmBmOeaXHHOXo89P9afN3jX3wd82MvDqBGCy2LURe-vTH45zKSVlmXtz5H74zh3--wJmvb6ZVzn_4phvMRjcxtzj8y2bfwfVIOoK-E-CrbRm</recordid><startdate>201011</startdate><enddate>201011</enddate><creator>Murray, Gerald L</creator><creator>Srikram, Amporn</creator><creator>Henry, Rebekah</creator><creator>Hartskeerl, Rudy A</creator><creator>Sermswan, Rasana W</creator><creator>Adler, Ben</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>FBQ</scope><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><scope>7X8</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope></search><sort><creationdate>201011</creationdate><title>Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence</title><author>Murray, Gerald L ; Srikram, Amporn ; Henry, Rebekah ; Hartskeerl, Rudy A ; Sermswan, Rasana W ; Adler, Ben</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5970-96a481bed1f24069e0ffe8ac2c4914f188ce3f22cc250d2ba92c05ee181da33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Bacteria</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Cricetinae</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Leptospira interrogans</topic><topic>Leptospira interrogans - genetics</topic><topic>Leptospira interrogans - metabolism</topic><topic>Leptospira interrogans - pathogenicity</topic><topic>Leptospirosis - microbiology</topic><topic>Lipopolysaccharides - deficiency</topic><topic>Lipopolysaccharides - genetics</topic><topic>Membranes</topic><topic>Mesocricetus</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Molecular biology</topic><topic>Mutagenesis, Insertional</topic><topic>Mutation</topic><topic>Pathogenesis</topic><topic>Proteins</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murray, Gerald L</creatorcontrib><creatorcontrib>Srikram, Amporn</creatorcontrib><creatorcontrib>Henry, Rebekah</creatorcontrib><creatorcontrib>Hartskeerl, Rudy A</creatorcontrib><creatorcontrib>Sermswan, Rasana W</creatorcontrib><creatorcontrib>Adler, Ben</creatorcontrib><collection>AGRIS</collection><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><collection>MEDLINE - Academic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Molecular microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murray, Gerald L</au><au>Srikram, Amporn</au><au>Henry, Rebekah</au><au>Hartskeerl, Rudy A</au><au>Sermswan, Rasana W</au><au>Adler, Ben</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence</atitle><jtitle>Molecular microbiology</jtitle><addtitle>Mol Microbiol</addtitle><date>2010-11</date><risdate>2010</risdate><volume>78</volume><issue>3</issue><spage>701</spage><epage>709</epage><pages>701-709</pages><issn>0950-382X</issn><eissn>1365-2958</eissn><abstract>Leptospira interrogans is the causative agent of leptospirosis. Lipopolysaccharide (LPS) is the major outer membrane component of L. interrogans. It is the dominant antigen recognized during infection and the basis for serological classification. The structure of LPS and its role in pathogenesis are unknown. We describe two defined mutants of L. interrogans serovar Manilae with transposon insertions in the LPS locus. Mutant M895 was disrupted in gene la1641 encoding a protein with no known homologues. M1352 was disrupted in a gene unique to serovar Manilae also encoding a protein of unknown function. M895 produced truncated LPS while M1352 showed little or no change in LPS molecular mass. Both mutants showed altered agglutination titres against rabbit antiserum and against a panel of LPS‐specific monoclonal antibodies. The mutants were severely attenuated in virulence via the intraperitoneal route of infection, and were cleared from the host animal by 3 days after infection. M895 was also highly attenuated via the mucosal infection route. Resistance to complement in human serum was unaltered for both mutants. While complementation of mutants was not possible, the attenuation of two independently derived LPS mutants demonstrates for the first time that LPS plays an essential role leptospiral virulence.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>20807198</pmid><doi>10.1111/j.1365-2958.2010.07360.x</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Cricetinae Fundamental and applied biological sciences. Psychology Humans Leptospira interrogans Leptospira interrogans - genetics Leptospira interrogans - metabolism Leptospira interrogans - pathogenicity Leptospirosis - microbiology Lipopolysaccharides - deficiency Lipopolysaccharides - genetics Membranes Mesocricetus Microbiology Miscellaneous Molecular biology Mutagenesis, Insertional Mutation Pathogenesis Proteins Virulence |
| title | Mutations affecting Leptospira interrogans lipopolysaccharide attenuate virulence |
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