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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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: 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
Format: Article in Journal/Newspaper
Language:English
Published: HAL CCSD 2007
Subjects:
Online Access:https://hal.archives-ouvertes.fr/hal-00258926
https://doi.org/10.1073/pnas.0702281104
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spelling ftccsdartic:oai:HAL:hal-00258926v1 2023-05-15T15:58:07+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 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 2007-11-06 https://hal.archives-ouvertes.fr/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.archives-ouvertes.fr/hal-00258926 doi:10.1073/pnas.0702281104 PUBMED: 17965238 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-00258926 Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 2007, 104 (45), pp.17759-64. ⟨10.1073/pnas.0702281104⟩ MESH: Amino Acid Sequence MESH: Animals 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 MESH: Crassostrea MESH: DNA Complementary MESH: Escherichia coli MESH: Expressed Sequence Tags MESH: Invertebrates [SDV.BC]Life Sciences [q-bio]/Cellular Biology info:eu-repo/semantics/article Journal articles 2007 ftccsdartic https://doi.org/10.1073/pnas.0702281104 2021-10-17T02:11:19Z 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 MESH: Amino Acid Sequence
MESH: Animals
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
MESH: Crassostrea
MESH: DNA
Complementary
MESH: Escherichia coli
MESH: Expressed Sequence Tags
MESH: Invertebrates
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
spellingShingle MESH: Amino Acid Sequence
MESH: Animals
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
MESH: Crassostrea
MESH: DNA
Complementary
MESH: Escherichia coli
MESH: Expressed Sequence Tags
MESH: Invertebrates
[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: 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
MESH: Crassostrea
MESH: DNA
Complementary
MESH: Escherichia coli
MESH: Expressed Sequence Tags
MESH: Invertebrates
[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
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-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.archives-ouvertes.fr/hal-00258926
Proceedings of the National Academy of Sciences of the United States of America , National Academy of Sciences, 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.archives-ouvertes.fr/hal-00258926
doi:10.1073/pnas.0702281104
PUBMED: 17965238
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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