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...
Published in: | Proceedings of the National Academy of Sciences |
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Online Access: | https://hal.science/hal-00258926 https://doi.org/10.1073/pnas.0702281104 |
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ftunimontpellier:oai:HAL:hal-00258926v1 2024-04-28T08:16:30+00:00 Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI 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 Institut de Recherche en Infectiologie de Montpellier (IRIM) Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) Laboratoire d'Ecologie Numérique et d'Ecotoxicologie Université de Lille, Sciences et Technologies-Centre National de la Recherche Scientifique (CNRS) Atheris Laboratories Laboratoire Adaptation et pathogénie des micro-organismes Grenoble (LAPM) Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS) 2007-11-06 https://hal.science/hal-00258926 https://doi.org/10.1073/pnas.0702281104 en eng HAL CCSD National Academy of Sciences info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0702281104 info:eu-repo/semantics/altIdentifier/pmid/17965238 hal-00258926 https://hal.science/hal-00258926 doi:10.1073/pnas.0702281104 PUBMED: 17965238 PUBMEDCENTRAL: PMC2077063 ISSN: 0027-8424 EISSN: 1091-6490 Proceedings of the National Academy of Sciences of the United States of America https://hal.science/hal-00258926 Proceedings of the National Academy of Sciences of the United States of America, 2007, 104 (45), pp.17759-64. ⟨10.1073/pnas.0702281104⟩ MESH: Amino Acid Sequence MESH: Animals MESH: Crassostrea MESH: DNA Complementary MESH: Escherichia coli MESH: Expressed Sequence Tags MESH: Invertebrates MESH: Membrane Proteins MESH: Molecular Sequence Data MESH: Ostreidae MESH: Sequence Alignment MESH: Sequence Homology Amino Acid MESH: Antimicrobial Cationic Peptides MESH: Blood Proteins MESH: Cell Membrane Permeability [SDV.BC]Life Sciences [q-bio]/Cellular Biology info:eu-repo/semantics/article Journal articles 2007 ftunimontpellier https://doi.org/10.1073/pnas.0702281104 2024-04-10T14:35:50Z 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. Article in Journal/Newspaper Crassostrea gigas Université de Montpellier: HAL Proceedings of the National Academy of Sciences 104 45 17759 17764 |
institution |
Open Polar |
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Université de Montpellier: HAL |
op_collection_id |
ftunimontpellier |
language |
English |
topic |
MESH: Amino Acid Sequence MESH: Animals MESH: Crassostrea MESH: DNA Complementary MESH: Escherichia coli MESH: Expressed Sequence Tags MESH: Invertebrates MESH: Membrane Proteins MESH: Molecular Sequence Data MESH: Ostreidae MESH: Sequence Alignment MESH: Sequence Homology Amino Acid MESH: Antimicrobial Cationic Peptides MESH: Blood Proteins MESH: Cell Membrane Permeability [SDV.BC]Life Sciences [q-bio]/Cellular Biology |
spellingShingle |
MESH: Amino Acid Sequence MESH: Animals MESH: Crassostrea MESH: DNA Complementary MESH: Escherichia coli MESH: Expressed Sequence Tags MESH: Invertebrates MESH: Membrane Proteins MESH: Molecular Sequence Data MESH: Ostreidae MESH: Sequence Alignment MESH: Sequence Homology Amino Acid MESH: Antimicrobial Cationic Peptides MESH: Blood Proteins MESH: Cell Membrane Permeability [SDV.BC]Life Sciences [q-bio]/Cellular Biology 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 Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
topic_facet |
MESH: Amino Acid Sequence MESH: Animals MESH: Crassostrea MESH: DNA Complementary MESH: Escherichia coli MESH: Expressed Sequence Tags MESH: Invertebrates MESH: Membrane Proteins MESH: Molecular Sequence Data MESH: Ostreidae MESH: Sequence Alignment MESH: Sequence Homology Amino Acid MESH: Antimicrobial Cationic Peptides MESH: Blood Proteins MESH: Cell Membrane Permeability [SDV.BC]Life Sciences [q-bio]/Cellular Biology |
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. |
author2 |
Institut de Recherche en Infectiologie de Montpellier (IRIM) Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) Laboratoire d'Ecologie Numérique et d'Ecotoxicologie Université de Lille, Sciences et Technologies-Centre National de la Recherche Scientifique (CNRS) Atheris Laboratories Laboratoire Adaptation et pathogénie des micro-organismes Grenoble (LAPM) Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS) |
format |
Article in Journal/Newspaper |
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_facet |
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 |
Gonzalez, Marcelo |
title |
Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
title_short |
Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
title_full |
Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
title_fullStr |
Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
title_full_unstemmed |
Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI |
title_sort |
evidence of a bactericidal permeability increasing protein in an invertebrate, the crassostrea gigas cg-bpi |
publisher |
HAL CCSD |
publishDate |
2007 |
url |
https://hal.science/hal-00258926 https://doi.org/10.1073/pnas.0702281104 |
genre |
Crassostrea gigas |
genre_facet |
Crassostrea gigas |
op_source |
ISSN: 0027-8424 EISSN: 1091-6490 Proceedings of the National Academy of Sciences of the United States of America https://hal.science/hal-00258926 Proceedings of the National Academy of Sciences of the United States of America, 2007, 104 (45), pp.17759-64. ⟨10.1073/pnas.0702281104⟩ |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0702281104 info:eu-repo/semantics/altIdentifier/pmid/17965238 hal-00258926 https://hal.science/hal-00258926 doi:10.1073/pnas.0702281104 PUBMED: 17965238 PUBMEDCENTRAL: PMC2077063 |
op_doi |
https://doi.org/10.1073/pnas.0702281104 |
container_title |
Proceedings of the National Academy of Sciences |
container_volume |
104 |
container_issue |
45 |
container_start_page |
17759 |
op_container_end_page |
17764 |
_version_ |
1797581613529300992 |