title: Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI.
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. To our knowledge, this is the first characterization of a BPI in an invertebrate.
authors.affiliation: Ifremer, Centre National de la Recherche Scientifique, Université Montpellier 2, Unité Mixte de Recherche 5119, Ecosystèmes Lagunaires, Place E. Bataillon, CC80, 34095 Montpellier Cedex 5, France.
authors.forename: Marcelo
authors.initials: M
authors.lastname: Gonzalez
authors.forename: Yannick
authors.initials: Y
authors.lastname: Gueguen
authors.forename: Delphine
authors.initials: D
authors.lastname: Destoumieux-Garzón
authors.forename: Bernard
authors.initials: B
authors.lastname: Romestand
authors.forename: Julie
authors.initials: J
authors.lastname: Fievet
authors.forename: Martine
authors.initials: M
authors.lastname: Pugnière
authors.forename: Françoise
authors.initials: F
authors.lastname: Roquet
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Escoubas
authors.forename: Franck
authors.initials: F
authors.lastname: Vandenbulcke
authors.forename: Ofer
authors.initials: O
authors.lastname: Levy
authors.forename: Laure
authors.initials: L
authors.lastname: Sauné
authors.forename: Philippe
authors.initials: P
authors.lastname: Bulet
authors.forename: Evelyne
authors.initials: E
authors.lastname: Bachère
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D001798:Blood Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D002463:Cell Membrane Permeability; D049896:Crassostrea / Q000382:microbiology / Q000502:physiology*; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli / Q000502:physiology*; D020224:Expressed Sequence Tags; D007448:Invertebrates / Q000382:microbiology / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D010125:Ostreidae / Q000235:genetics / Q000382:microbiology / Q000502:physiology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D018076:DNA, Complementary; D008565:Membrane Proteins; C021623:bactericidal permeability increasing protein