The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans
Leptospirosis is a potentially fatal zoonotic disease in humans and animals caused by pathogenic spirochetes, such as Leptospira interrogans. The mode of transmission is commonly limited to the exposure of mucous membrane or damaged skin to water contaminated by leptospires shed in the urine of carr...
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| Veröffentlicht in: | PloS one 2011-02, Vol.6 (2), p.e16879 |
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| description | Leptospirosis is a potentially fatal zoonotic disease in humans and animals caused by pathogenic spirochetes, such as Leptospira interrogans. The mode of transmission is commonly limited to the exposure of mucous membrane or damaged skin to water contaminated by leptospires shed in the urine of carriers, such as rats. Infection occurs during seasonal flooding of impoverished tropical urban habitats with large rat populations, but also during recreational activity in open water, suggesting it is very efficient. LigA and LigB are surface localized proteins in pathogenic Leptospira strains with properties that could facilitate the infection of damaged skin. Their expression is rapidly induced by the increase in osmolarity encountered by leptospires upon transition from water to host. In addition, the immunoglobulin-like repeats of the Lig proteins bind proteins that mediate attachment to host tissue, such as fibronectin, fibrinogen, collagens, laminin, and elastin, some of which are important in cutaneous wound healing and repair. Hemostasis is critical in a fresh injury, where fibrinogen from damaged vasculature mediates coagulation. We show that fibrinogen binding by recombinant LigB inhibits fibrin formation, which could aid leptospiral entry into the circulation, dissemination, and further infection by impairing healing. LigB also binds fibroblast fibronectin and type III collagen, two proteins prevalent in wound repair, thus potentially enhancing leptospiral adhesion to skin openings. LigA or LigB expression by transformation of a nonpathogenic saprophyte, L. biflexa, enhances bacterial adhesion to fibrinogen. Our results suggest that by binding homeostatic proteins found in cutaneous wounds, LigB could facilitate leptospirosis transmission. Both fibronectin and fibrinogen binding have been mapped to an overlapping domain in LigB comprising repeats 9-11, with repeat 11 possibly enhancing binding by a conformational effect. Leptospirosis patient antibodies react with the LigB domain, suggesting applications in diagnosis and vaccines that are currently limited by the strain-specific leptospiral lipopolysaccharide coats. |
| doi_str_mv | 10.1371/journal.pone.0016879 |
| format | Article |
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The mode of transmission is commonly limited to the exposure of mucous membrane or damaged skin to water contaminated by leptospires shed in the urine of carriers, such as rats. Infection occurs during seasonal flooding of impoverished tropical urban habitats with large rat populations, but also during recreational activity in open water, suggesting it is very efficient. LigA and LigB are surface localized proteins in pathogenic Leptospira strains with properties that could facilitate the infection of damaged skin. Their expression is rapidly induced by the increase in osmolarity encountered by leptospires upon transition from water to host. In addition, the immunoglobulin-like repeats of the Lig proteins bind proteins that mediate attachment to host tissue, such as fibronectin, fibrinogen, collagens, laminin, and elastin, some of which are important in cutaneous wound healing and repair. Hemostasis is critical in a fresh injury, where fibrinogen from damaged vasculature mediates coagulation. We show that fibrinogen binding by recombinant LigB inhibits fibrin formation, which could aid leptospiral entry into the circulation, dissemination, and further infection by impairing healing. LigB also binds fibroblast fibronectin and type III collagen, two proteins prevalent in wound repair, thus potentially enhancing leptospiral adhesion to skin openings. LigA or LigB expression by transformation of a nonpathogenic saprophyte, L. biflexa, enhances bacterial adhesion to fibrinogen. Our results suggest that by binding homeostatic proteins found in cutaneous wounds, LigB could facilitate leptospirosis transmission. Both fibronectin and fibrinogen binding have been mapped to an overlapping domain in LigB comprising repeats 9-11, with repeat 11 possibly enhancing binding by a conformational effect. Leptospirosis patient antibodies react with the LigB domain, suggesting applications in diagnosis and vaccines that are currently limited by the strain-specific leptospiral lipopolysaccharide coats.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0016879</identifier><identifier>PMID: 21347378</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adhesins, Bacterial - chemistry ; Adhesins, Bacterial - metabolism ; Adhesion ; AIDS vaccines ; Animal bites ; Animal diseases ; Antibodies ; Antibodies, Bacterial - immunology ; Bacteria ; Bacterial Adhesion ; Binding ; Biology ; Coagulation ; Collagen ; Collagen (type III) ; E coli ; Elastin ; Epidemiology ; Escherichia coli ; Extracellular matrix ; Fibrin ; Fibrin - metabolism ; Fibrinogen ; Fibrinogen - metabolism ; Fibronectin ; Fibronectins ; Fibronectins - metabolism ; Flooding ; Gram-negative bacteria ; Health aspects ; Hemostasis ; Hemostatics ; Humans ; Immunoglobulins ; Infection ; Infections ; Laminin ; Leptospira ; Leptospira interrogans ; Leptospira interrogans - genetics ; Leptospira interrogans - immunology ; Leptospira interrogans - metabolism ; Leptospira interrogans - pathogenicity ; Leptospirosis ; Leptospirosis - immunology ; Leptospirosis - metabolism ; Leptospirosis - microbiology ; Lipopolysaccharides ; Medicine ; Mitogens ; Osmolarity ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; R&D ; Rats ; Repair ; Research & development ; Skin ; Skin Diseases, Bacterial - metabolism ; Skin Diseases, Bacterial - microbiology ; Spirochetes ; Staphylococcus aureus ; Transformation ; Transformation, Bacterial ; Urine ; Vaccines ; Veterans ; Water damage ; Water pollution ; Wound Healing ; Zoonoses</subject><ispartof>PloS one, 2011-02, Vol.6 (2), p.e16879</ispartof><rights>COPYRIGHT 2011 Public Library of Science</rights><rights>2011. This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c691t-a6f928765026e69b5a18854aa94fe98d0ac1a8aaa66d2ebbd21b453402d540b43</citedby><cites>FETCH-LOGICAL-c691t-a6f928765026e69b5a18854aa94fe98d0ac1a8aaa66d2ebbd21b453402d540b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3036719/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3036719/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21347378$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ho, Paulo</contributor><creatorcontrib>Choy, Henry A</creatorcontrib><creatorcontrib>Kelley, Melissa M</creatorcontrib><creatorcontrib>Croda, Julio</creatorcontrib><creatorcontrib>Matsunaga, James</creatorcontrib><creatorcontrib>Babbitt, Jane T</creatorcontrib><creatorcontrib>Ko, Albert I</creatorcontrib><creatorcontrib>Picardeau, Mathieu</creatorcontrib><creatorcontrib>Haake, David A</creatorcontrib><title>The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Leptospirosis is a potentially fatal zoonotic disease in humans and animals caused by pathogenic spirochetes, such as Leptospira interrogans. The mode of transmission is commonly limited to the exposure of mucous membrane or damaged skin to water contaminated by leptospires shed in the urine of carriers, such as rats. Infection occurs during seasonal flooding of impoverished tropical urban habitats with large rat populations, but also during recreational activity in open water, suggesting it is very efficient. LigA and LigB are surface localized proteins in pathogenic Leptospira strains with properties that could facilitate the infection of damaged skin. Their expression is rapidly induced by the increase in osmolarity encountered by leptospires upon transition from water to host. In addition, the immunoglobulin-like repeats of the Lig proteins bind proteins that mediate attachment to host tissue, such as fibronectin, fibrinogen, collagens, laminin, and elastin, some of which are important in cutaneous wound healing and repair. Hemostasis is critical in a fresh injury, where fibrinogen from damaged vasculature mediates coagulation. We show that fibrinogen binding by recombinant LigB inhibits fibrin formation, which could aid leptospiral entry into the circulation, dissemination, and further infection by impairing healing. LigB also binds fibroblast fibronectin and type III collagen, two proteins prevalent in wound repair, thus potentially enhancing leptospiral adhesion to skin openings. LigA or LigB expression by transformation of a nonpathogenic saprophyte, L. biflexa, enhances bacterial adhesion to fibrinogen. Our results suggest that by binding homeostatic proteins found in cutaneous wounds, LigB could facilitate leptospirosis transmission. Both fibronectin and fibrinogen binding have been mapped to an overlapping domain in LigB comprising repeats 9-11, with repeat 11 possibly enhancing binding by a conformational effect. Leptospirosis patient antibodies react with the LigB domain, suggesting applications in diagnosis and vaccines that are currently limited by the strain-specific leptospiral lipopolysaccharide coats.</description><subject>Adhesins, Bacterial - chemistry</subject><subject>Adhesins, Bacterial - metabolism</subject><subject>Adhesion</subject><subject>AIDS vaccines</subject><subject>Animal bites</subject><subject>Animal diseases</subject><subject>Antibodies</subject><subject>Antibodies, Bacterial - immunology</subject><subject>Bacteria</subject><subject>Bacterial Adhesion</subject><subject>Binding</subject><subject>Biology</subject><subject>Coagulation</subject><subject>Collagen</subject><subject>Collagen (type III)</subject><subject>E coli</subject><subject>Elastin</subject><subject>Epidemiology</subject><subject>Escherichia coli</subject><subject>Extracellular matrix</subject><subject>Fibrin</subject><subject>Fibrin - metabolism</subject><subject>Fibrinogen</subject><subject>Fibrinogen - metabolism</subject><subject>Fibronectin</subject><subject>Fibronectins</subject><subject>Fibronectins - metabolism</subject><subject>Flooding</subject><subject>Gram-negative bacteria</subject><subject>Health aspects</subject><subject>Hemostasis</subject><subject>Hemostatics</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Infection</subject><subject>Infections</subject><subject>Laminin</subject><subject>Leptospira</subject><subject>Leptospira interrogans</subject><subject>Leptospira interrogans - genetics</subject><subject>Leptospira interrogans - immunology</subject><subject>Leptospira interrogans - metabolism</subject><subject>Leptospira interrogans - pathogenicity</subject><subject>Leptospirosis</subject><subject>Leptospirosis - immunology</subject><subject>Leptospirosis - metabolism</subject><subject>Leptospirosis - microbiology</subject><subject>Lipopolysaccharides</subject><subject>Medicine</subject><subject>Mitogens</subject><subject>Osmolarity</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>R&D</subject><subject>Rats</subject><subject>Repair</subject><subject>Research & development</subject><subject>Skin</subject><subject>Skin Diseases, Bacterial - metabolism</subject><subject>Skin Diseases, Bacterial - microbiology</subject><subject>Spirochetes</subject><subject>Staphylococcus aureus</subject><subject>Transformation</subject><subject>Transformation, Bacterial</subject><subject>Urine</subject><subject>Vaccines</subject><subject>Veterans</subject><subject>Water damage</subject><subject>Water pollution</subject><subject>Wound Healing</subject><subject>Zoonoses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99u0zAUxiMEYqPwBggiIYG4aLFjx4lvkMbEn0qVJsHg1jpxThJXaZzZDrB34KFx125q0S5QLhLbv-9z_B2fJHlOyYKygr5b28kN0C9GO-CCECrKQj5ITqlk2VxkhD08-D5Jnni_JiRnpRCPk5OMMl6wojxN_lx2mG6mPphmGnQwNlqmK9N-SKHu0JshrcxQ-7SzG7Q-QDA6HZ0NaAaf_jKhS8c4GIKJMmd79GmU6CnAgHbaDhq8cU2r63SE0NkWh2ixwjFYPxoHEQnonG1h8E-TRw30Hp_t37Pk-6ePl-df5quLz8vzs9VcC0nDHEQjs7IQOckEClnlQMsy5wCSNyjLmoCmUAKAEHWGVVVntOI54ySrc04qzmbJy53v2Fuv9kF6RTOZCUGzGNgsWe6I2sJajc5swF0rC0bdTFjXKnAxix6VJCVSTnhVa8JroivKG02wAamZaDRGr_f73aZqg7WOaTnoj0yPVwbTqdb-VIwwUcQazpI3ewNnryb0QW2M19j3u5BVmTMpWVGISL76h7z_cHuqhfj_sUQ2bqu3nuqMF0KSXMgiUot7qPjUuDE6XrrGxPkjwdsjQWQC_g4tTN6r5bev_89e_DhmXx-wHUIfOm_7aXut_DHId6B21nuHzV3GlKhtz9ymobY9o_Y9E2UvDutzJ7ptEvYXDj0VwA</recordid><startdate>20110209</startdate><enddate>20110209</enddate><creator>Choy, Henry A</creator><creator>Kelley, Melissa M</creator><creator>Croda, Julio</creator><creator>Matsunaga, James</creator><creator>Babbitt, Jane T</creator><creator>Ko, Albert I</creator><creator>Picardeau, Mathieu</creator><creator>Haake, David A</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110209</creationdate><title>The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans</title><author>Choy, Henry A ; Kelley, Melissa M ; Croda, Julio ; Matsunaga, James ; Babbitt, Jane T ; Ko, Albert I ; Picardeau, Mathieu ; Haake, David A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c691t-a6f928765026e69b5a18854aa94fe98d0ac1a8aaa66d2ebbd21b453402d540b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adhesins, Bacterial - 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Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choy, Henry A</au><au>Kelley, Melissa M</au><au>Croda, Julio</au><au>Matsunaga, James</au><au>Babbitt, Jane T</au><au>Ko, Albert I</au><au>Picardeau, Mathieu</au><au>Haake, David A</au><au>Ho, Paulo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2011-02-09</date><risdate>2011</risdate><volume>6</volume><issue>2</issue><spage>e16879</spage><pages>e16879-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Leptospirosis is a potentially fatal zoonotic disease in humans and animals caused by pathogenic spirochetes, such as Leptospira interrogans. The mode of transmission is commonly limited to the exposure of mucous membrane or damaged skin to water contaminated by leptospires shed in the urine of carriers, such as rats. Infection occurs during seasonal flooding of impoverished tropical urban habitats with large rat populations, but also during recreational activity in open water, suggesting it is very efficient. LigA and LigB are surface localized proteins in pathogenic Leptospira strains with properties that could facilitate the infection of damaged skin. Their expression is rapidly induced by the increase in osmolarity encountered by leptospires upon transition from water to host. In addition, the immunoglobulin-like repeats of the Lig proteins bind proteins that mediate attachment to host tissue, such as fibronectin, fibrinogen, collagens, laminin, and elastin, some of which are important in cutaneous wound healing and repair. Hemostasis is critical in a fresh injury, where fibrinogen from damaged vasculature mediates coagulation. We show that fibrinogen binding by recombinant LigB inhibits fibrin formation, which could aid leptospiral entry into the circulation, dissemination, and further infection by impairing healing. LigB also binds fibroblast fibronectin and type III collagen, two proteins prevalent in wound repair, thus potentially enhancing leptospiral adhesion to skin openings. LigA or LigB expression by transformation of a nonpathogenic saprophyte, L. biflexa, enhances bacterial adhesion to fibrinogen. Our results suggest that by binding homeostatic proteins found in cutaneous wounds, LigB could facilitate leptospirosis transmission. Both fibronectin and fibrinogen binding have been mapped to an overlapping domain in LigB comprising repeats 9-11, with repeat 11 possibly enhancing binding by a conformational effect. Leptospirosis patient antibodies react with the LigB domain, suggesting applications in diagnosis and vaccines that are currently limited by the strain-specific leptospiral lipopolysaccharide coats.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21347378</pmid><doi>10.1371/journal.pone.0016879</doi><tpages>e16879</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2011-02, Vol.6 (2), p.e16879 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1292661220 |
| 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; Free Full-Text Journals in Chemistry |
| subjects | Adhesins, Bacterial - chemistry Adhesins, Bacterial - metabolism Adhesion AIDS vaccines Animal bites Animal diseases Antibodies Antibodies, Bacterial - immunology Bacteria Bacterial Adhesion Binding Biology Coagulation Collagen Collagen (type III) E coli Elastin Epidemiology Escherichia coli Extracellular matrix Fibrin Fibrin - metabolism Fibrinogen Fibrinogen - metabolism Fibronectin Fibronectins Fibronectins - metabolism Flooding Gram-negative bacteria Health aspects Hemostasis Hemostatics Humans Immunoglobulins Infection Infections Laminin Leptospira Leptospira interrogans Leptospira interrogans - genetics Leptospira interrogans - immunology Leptospira interrogans - metabolism Leptospira interrogans - pathogenicity Leptospirosis Leptospirosis - immunology Leptospirosis - metabolism Leptospirosis - microbiology Lipopolysaccharides Medicine Mitogens Osmolarity Protein Binding Protein Structure, Tertiary Proteins R&D Rats Repair Research & development Skin Skin Diseases, Bacterial - metabolism Skin Diseases, Bacterial - microbiology Spirochetes Staphylococcus aureus Transformation Transformation, Bacterial Urine Vaccines Veterans Water damage Water pollution Wound Healing Zoonoses |
| title | The multifunctional LigB adhesin binds homeostatic proteins with potential roles in cutaneous infection by pathogenic Leptospira interrogans |
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