Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg -BPI

International audience 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 Escheric...

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Published in:Proceedings of the National Academy of Sciences
Main Authors: 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
Other Authors: Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire Grenoble (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)
Format: Article in Journal/Newspaper
Language:English
Published: HAL CCSD 2007
Subjects:
Online Access:https://hal.archives-ouvertes.fr/hal-03828696
https://doi.org/10.1073/pnas.0702281104
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spelling ftccsdartic:oai:HAL:hal-03828696v1 2023-05-15T15:57:52+02:00 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 Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB) Centre Hospitalier Universitaire Grenoble (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA) 2007-11-06 https://hal.archives-ouvertes.fr/hal-03828696 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 hal-03828696 https://hal.archives-ouvertes.fr/hal-03828696 doi:10.1073/pnas.0702281104 ISSN: 0027-8424 EISSN: 1091-6490 Proceedings of the National Academy of Sciences of the United States of America https://hal.archives-ouvertes.fr/hal-03828696 Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2007, 104 (45), pp.17759-17764. ⟨10.1073/pnas.0702281104⟩ [SDV]Life Sciences [q-bio] info:eu-repo/semantics/article Journal articles 2007 ftccsdartic https://doi.org/10.1073/pnas.0702281104 2022-10-29T23:14:58Z International audience 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 Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe) Proceedings of the National Academy of Sciences 104 45 17759 17764
institution Open Polar
collection Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe)
op_collection_id ftccsdartic
language English
topic [SDV]Life Sciences [q-bio]
spellingShingle [SDV]Life Sciences [q-bio]
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 [SDV]Life Sciences [q-bio]
description International audience 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 Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB)
Centre Hospitalier Universitaire Grenoble (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)
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.archives-ouvertes.fr/hal-03828696
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.archives-ouvertes.fr/hal-03828696
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2007, 104 (45), pp.17759-17764. ⟨10.1073/pnas.0702281104⟩
op_relation info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0702281104
hal-03828696
https://hal.archives-ouvertes.fr/hal-03828696
doi:10.1073/pnas.0702281104
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
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