Evidence of a Bactericidal Permeability Increasing Protein in an Invertebrate, the Crassostrea gigas Cg-BPI
A cDNA sequence with homologies to members of the LPS-binding protein and bactericidal/permeability-increasing protein (BPI) family was identified in the oyster Crassostrea gigas. The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increas...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-11, Vol.104 (45), p.17759-17764 |
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| creator | Gonzalez, Marcelo Gueguen, Yannick Destoumieux-Garzón, Delphine Romestand, Bernard Fievet, Julie Pugnière, Martine Roquet, Françoise Escoubas, Jean-Michel Vandenbulcke, Franck Levy, Ofer Sauné, Laure Bulet, Philippe Bachère, Evelyne |
| description | A cDNA sequence with homologies to members of the LPS-binding protein and bactericidal/permeability-increasing protein (BPI) family was identified in the oyster Crassostrea gigas. The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increase the permeability of the bacterial cytoplasmic membrane. This indicated that it is a BPI rather than an LPS-binding protein. By in situ hybridization, the expression of the C. gigas BPI (Cg-bpi) was found to be induced in hemocytes after oyster bacterial challenge and to be constitutive in various epithelia of unchallenged oysters. Thus, Cg-bpi transcripts were detected in the epithelial cells of tissues/organs in contact with the external environment (mantle, gills, digestive tract, digestive gland diverticula, and gonad follicles). Therefore, Cg-BPI, whose expression profile and biological properties are reminiscent of mammalian BPIs, may provide a first line of defense against potential bacterial invasion. To our knowledge, this is the first characterization of a BPI in an invertebrate. |
| doi_str_mv | 10.1073/pnas.0702281104 |
| format | Article |
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The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increase the permeability of the bacterial cytoplasmic membrane. This indicated that it is a BPI rather than an LPS-binding protein. By in situ hybridization, the expression of the C. gigas BPI (Cg-bpi) was found to be induced in hemocytes after oyster bacterial challenge and to be constitutive in various epithelia of unchallenged oysters. Thus, Cg-bpi transcripts were detected in the epithelial cells of tissues/organs in contact with the external environment (mantle, gills, digestive tract, digestive gland diverticula, and gonad follicles). Therefore, Cg-BPI, whose expression profile and biological properties are reminiscent of mammalian BPIs, may provide a first line of defense against potential bacterial invasion. To our knowledge, this is the first characterization of a BPI in an invertebrate.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0702281104</identifier><identifier>PMID: 17965238</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Animals ; Antibacterials ; Antimicrobial Cationic Peptides ; Antimicrobial Cationic Peptides - chemistry ; Antimicrobial Cationic Peptides - genetics ; Antimicrobial Cationic Peptides - metabolism ; Antimicrobials ; Bacterial proteins ; Binding sites ; Biological Sciences ; Blood Proteins ; Blood Proteins - chemistry ; Blood Proteins - genetics ; Blood Proteins - metabolism ; Cell Membrane Permeability ; Cellular Biology ; Complementary DNA ; Crassostrea ; Crassostrea - microbiology ; Crassostrea - physiology ; Crassostrea gigas ; Deoxyribonucleic acid ; DNA ; DNA, Complementary ; DNA, Complementary - genetics ; E coli ; Escherichia coli ; Escherichia coli - physiology ; Expressed Sequence Tags ; Genes ; Hemocytes ; Invertebrata ; Invertebrates ; Invertebrates - microbiology ; Invertebrates - physiology ; Life Sciences ; Lipids ; Marine ; Membrane Proteins ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Molecular Sequence Data ; Ostreidae ; Ostreidae - genetics ; Ostreidae - microbiology ; Ostreidae - physiology ; Oysters ; Permeability ; Proteins ; Recombinant proteins ; Sequence Alignment ; Sequence Homology, Amino Acid</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-11, Vol.104 (45), p.17759-17764</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Nov 6, 2007</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2007 by The National Academy of Sciences of the USA 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-6a1c71030b59078142b6f7dc162fbcbd557e3ae8243829a1cb641bbd0dd0ad7f3</citedby><cites>FETCH-LOGICAL-c523t-6a1c71030b59078142b6f7dc162fbcbd557e3ae8243829a1cb641bbd0dd0ad7f3</cites><orcidid>0000-0002-8749-9582 ; 0000-0002-8793-9138 ; 0000-0002-6138-1148 ; 0000-0001-9016-265X ; 0000-0002-2049-2909</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/45.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25450316$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25450316$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17965238$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00258926$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Gonzalez, Marcelo</creatorcontrib><creatorcontrib>Gueguen, Yannick</creatorcontrib><creatorcontrib>Destoumieux-Garzón, Delphine</creatorcontrib><creatorcontrib>Romestand, Bernard</creatorcontrib><creatorcontrib>Fievet, Julie</creatorcontrib><creatorcontrib>Pugnière, Martine</creatorcontrib><creatorcontrib>Roquet, Françoise</creatorcontrib><creatorcontrib>Escoubas, Jean-Michel</creatorcontrib><creatorcontrib>Vandenbulcke, Franck</creatorcontrib><creatorcontrib>Levy, Ofer</creatorcontrib><creatorcontrib>Sauné, Laure</creatorcontrib><creatorcontrib>Bulet, Philippe</creatorcontrib><creatorcontrib>Bachère, Evelyne</creatorcontrib><title>Evidence of a Bactericidal Permeability Increasing Protein in an Invertebrate, the Crassostrea gigas Cg-BPI</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>A cDNA sequence with homologies to members of the LPS-binding protein and bactericidal/permeability-increasing protein (BPI) family was identified in the oyster Crassostrea gigas. The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increase the permeability of the bacterial cytoplasmic membrane. This indicated that it is a BPI rather than an LPS-binding protein. By in situ hybridization, the expression of the C. gigas BPI (Cg-bpi) was found to be induced in hemocytes after oyster bacterial challenge and to be constitutive in various epithelia of unchallenged oysters. Thus, Cg-bpi transcripts were detected in the epithelial cells of tissues/organs in contact with the external environment (mantle, gills, digestive tract, digestive gland diverticula, and gonad follicles). Therefore, Cg-BPI, whose expression profile and biological properties are reminiscent of mammalian BPIs, may provide a first line of defense against potential bacterial invasion. To our knowledge, this is the first characterization of a BPI in an invertebrate.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibacterials</subject><subject>Antimicrobial Cationic Peptides</subject><subject>Antimicrobial Cationic Peptides - chemistry</subject><subject>Antimicrobial Cationic Peptides - genetics</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Antimicrobials</subject><subject>Bacterial proteins</subject><subject>Binding sites</subject><subject>Biological Sciences</subject><subject>Blood Proteins</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - genetics</subject><subject>Blood Proteins - metabolism</subject><subject>Cell Membrane Permeability</subject><subject>Cellular Biology</subject><subject>Complementary DNA</subject><subject>Crassostrea</subject><subject>Crassostrea - microbiology</subject><subject>Crassostrea - physiology</subject><subject>Crassostrea gigas</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA, Complementary</subject><subject>DNA, Complementary - genetics</subject><subject>E coli</subject><subject>Escherichia coli</subject><subject>Escherichia coli - physiology</subject><subject>Expressed Sequence Tags</subject><subject>Genes</subject><subject>Hemocytes</subject><subject>Invertebrata</subject><subject>Invertebrates</subject><subject>Invertebrates - microbiology</subject><subject>Invertebrates - physiology</subject><subject>Life Sciences</subject><subject>Lipids</subject><subject>Marine</subject><subject>Membrane Proteins</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Ostreidae</subject><subject>Ostreidae - genetics</subject><subject>Ostreidae - microbiology</subject><subject>Ostreidae - physiology</subject><subject>Oysters</subject><subject>Permeability</subject><subject>Proteins</subject><subject>Recombinant proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0t2LEzEQAPBFFK-ePvukBB8Ewb2bfOwmeRHuyukdFOyDPodsdrZN3e7WJC3ef29Ky1UPRAgEkt9MhskUxWsKFxQkv9wMNl6ABMYUpSCeFBMKmpa10PC0mAAwWSrBxFnxIsYVAOhKwfPijEpdV4yrSfHjZudbHBySsSOWXFuXMHjnW9uTOYY12sb3Pt2Tu8EFtNEPCzIPY0I_kLzskC92GBI2wSb8SNISyTTYGMeYsicLv7CRTBfl9fzuZfGss33EV8f9vPj--ebb9Lacff1yN72alS7XlMraUicpcGgqDVJRwZq6k62jNesa17RVJZFbVExwxXTGTS1o07TQtmBb2fHz4tMh72bbrLF1OKRge7MJfm3DvRmtN3_fDH5pFuPOMJASap4TfDgkWD4Ku72amf1ZbmylNKt3NNv3x8fC-HOLMZm1jw773g44bqOplVCKav5fSLXkKv9ehu8ewdW4DUPuWC6QcqoFQEaXB-TCGGPA7qFOCmY_GmY_GuY0Gjni7Z9dOfnjLGRAjmAfeUonjKiykpU-NeafxHTbvk_4K2X75mBXMY3hAbNKVMBpzX8DCG3WkA</recordid><startdate>20071106</startdate><enddate>20071106</enddate><creator>Gonzalez, Marcelo</creator><creator>Gueguen, Yannick</creator><creator>Destoumieux-Garzón, Delphine</creator><creator>Romestand, Bernard</creator><creator>Fievet, Julie</creator><creator>Pugnière, Martine</creator><creator>Roquet, Françoise</creator><creator>Escoubas, Jean-Michel</creator><creator>Vandenbulcke, Franck</creator><creator>Levy, Ofer</creator><creator>Sauné, Laure</creator><creator>Bulet, Philippe</creator><creator>Bachère, Evelyne</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</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>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-8749-9582</orcidid><orcidid>https://orcid.org/0000-0002-8793-9138</orcidid><orcidid>https://orcid.org/0000-0002-6138-1148</orcidid><orcidid>https://orcid.org/0000-0001-9016-265X</orcidid><orcidid>https://orcid.org/0000-0002-2049-2909</orcidid></search><sort><creationdate>20071106</creationdate><title>Evidence of a Bactericidal Permeability Increasing Protein in an Invertebrate, the Crassostrea gigas Cg-BPI</title><author>Gonzalez, Marcelo ; Gueguen, Yannick ; Destoumieux-Garzón, Delphine ; Romestand, Bernard ; Fievet, Julie ; Pugnière, Martine ; Roquet, Françoise ; Escoubas, Jean-Michel ; Vandenbulcke, Franck ; Levy, Ofer ; Sauné, Laure ; Bulet, Philippe ; Bachère, Evelyne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-6a1c71030b59078142b6f7dc162fbcbd557e3ae8243829a1cb641bbd0dd0ad7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibacterials</topic><topic>Antimicrobial Cationic Peptides</topic><topic>Antimicrobial Cationic Peptides - chemistry</topic><topic>Antimicrobial Cationic Peptides - genetics</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Antimicrobials</topic><topic>Bacterial proteins</topic><topic>Binding sites</topic><topic>Biological Sciences</topic><topic>Blood Proteins</topic><topic>Blood Proteins - chemistry</topic><topic>Blood Proteins - genetics</topic><topic>Blood Proteins - metabolism</topic><topic>Cell Membrane Permeability</topic><topic>Cellular Biology</topic><topic>Complementary DNA</topic><topic>Crassostrea</topic><topic>Crassostrea - microbiology</topic><topic>Crassostrea - physiology</topic><topic>Crassostrea gigas</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA, Complementary</topic><topic>DNA, Complementary - genetics</topic><topic>E coli</topic><topic>Escherichia coli</topic><topic>Escherichia coli - physiology</topic><topic>Expressed Sequence Tags</topic><topic>Genes</topic><topic>Hemocytes</topic><topic>Invertebrata</topic><topic>Invertebrates</topic><topic>Invertebrates - microbiology</topic><topic>Invertebrates - physiology</topic><topic>Life Sciences</topic><topic>Lipids</topic><topic>Marine</topic><topic>Membrane Proteins</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Ostreidae</topic><topic>Ostreidae - genetics</topic><topic>Ostreidae - microbiology</topic><topic>Ostreidae - physiology</topic><topic>Oysters</topic><topic>Permeability</topic><topic>Proteins</topic><topic>Recombinant proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gonzalez, Marcelo</creatorcontrib><creatorcontrib>Gueguen, Yannick</creatorcontrib><creatorcontrib>Destoumieux-Garzón, Delphine</creatorcontrib><creatorcontrib>Romestand, Bernard</creatorcontrib><creatorcontrib>Fievet, Julie</creatorcontrib><creatorcontrib>Pugnière, Martine</creatorcontrib><creatorcontrib>Roquet, Françoise</creatorcontrib><creatorcontrib>Escoubas, Jean-Michel</creatorcontrib><creatorcontrib>Vandenbulcke, Franck</creatorcontrib><creatorcontrib>Levy, Ofer</creatorcontrib><creatorcontrib>Sauné, Laure</creatorcontrib><creatorcontrib>Bulet, Philippe</creatorcontrib><creatorcontrib>Bachère, Evelyne</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>Oceanic Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gonzalez, Marcelo</au><au>Gueguen, Yannick</au><au>Destoumieux-Garzón, Delphine</au><au>Romestand, Bernard</au><au>Fievet, Julie</au><au>Pugnière, Martine</au><au>Roquet, Françoise</au><au>Escoubas, Jean-Michel</au><au>Vandenbulcke, Franck</au><au>Levy, Ofer</au><au>Sauné, Laure</au><au>Bulet, Philippe</au><au>Bachère, Evelyne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evidence of a Bactericidal Permeability Increasing Protein in an Invertebrate, the Crassostrea gigas Cg-BPI</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2007-11-06</date><risdate>2007</risdate><volume>104</volume><issue>45</issue><spage>17759</spage><epage>17764</epage><pages>17759-17764</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A cDNA sequence with homologies to members of the LPS-binding protein and bactericidal/permeability-increasing protein (BPI) family was identified in the oyster Crassostrea gigas. The recombinant protein was found to bind LPS, to display bactericidal activity against Escherichia coli, and to increase the permeability of the bacterial cytoplasmic membrane. This indicated that it is a BPI rather than an LPS-binding protein. By in situ hybridization, the expression of the C. gigas BPI (Cg-bpi) was found to be induced in hemocytes after oyster bacterial challenge and to be constitutive in various epithelia of unchallenged oysters. Thus, Cg-bpi transcripts were detected in the epithelial cells of tissues/organs in contact with the external environment (mantle, gills, digestive tract, digestive gland diverticula, and gonad follicles). Therefore, Cg-BPI, whose expression profile and biological properties are reminiscent of mammalian BPIs, may provide a first line of defense against potential bacterial invasion. 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| subjects | Amino Acid Sequence Animals Antibacterials Antimicrobial Cationic Peptides Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - metabolism Antimicrobials Bacterial proteins Binding sites Biological Sciences Blood Proteins Blood Proteins - chemistry Blood Proteins - genetics Blood Proteins - metabolism Cell Membrane Permeability Cellular Biology Complementary DNA Crassostrea Crassostrea - microbiology Crassostrea - physiology Crassostrea gigas Deoxyribonucleic acid DNA DNA, Complementary DNA, Complementary - genetics E coli Escherichia coli Escherichia coli - physiology Expressed Sequence Tags Genes Hemocytes Invertebrata Invertebrates Invertebrates - microbiology Invertebrates - physiology Life Sciences Lipids Marine Membrane Proteins Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Molecular Sequence Data Ostreidae Ostreidae - genetics Ostreidae - microbiology Ostreidae - physiology Oysters Permeability Proteins Recombinant proteins Sequence Alignment Sequence Homology, Amino Acid |
| title | Evidence of a Bactericidal Permeability Increasing Protein in an Invertebrate, the Crassostrea gigas Cg-BPI |
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