FN Archimer Export Format
PT J
TI Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI
BT 
AF GONZALEZ, Marcelo
   GUEGUEN, Yannick
   DESTOUMIEUX GARZON, Delphine
   ROMESTAND, Bernard
   FIEVET, Julie
   PUGNIERE, M
   ROQUET, F
   ESCOUBAS, Jean-Michel
   VANDENBULCKE, F
   LEVY, O
   SAUNE, Laure
   BULET, P
   BACHERE, Evelyne
AS 1:6;2:1;3:2;4:6;5:1;6:2;7:2;8:2;9:3;10:4;11:1;12:5;13:1;
FF 1:;2:PDG-DOP-DCM-BOME-LALR;3:;4:;5:PDG-DOP-DCM-BOME-LALR;6:;7:;8:;9:;10:;11:PDG-DOP-DCM-BOME-LALR;12:;13:PDG-DOP-DCM-BOME;
C1 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
   Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5236, Centre d'Études d'Agents Pathogènes et Biotechnologie pour la Santé, Institut de Biologie, 34965 Montpellier, France
   Université des Sciences et Technologies de Lille, Ecologie Numérique et Ecotoxicologie,59655 Villeneuve d'Ascq, France;
   Children's Hospital Boston and Harvard Medical School, Boston, MA 02115
   Atheris Laboratories, CP314, 1233 Bernex-Geneva, Switzerland
C2 IFREMER, FRANCE
   CNRS, FRANCE
   UNIV LILLE, FRANCE;
   UNIV HAVARD, USA
   ATHERIS LABORATORIES, SWITZERLAND
   UNIV MONTPELLIER, FRANCE
SI MONTPELLIER
   PALAVAS
SE PDG-DOP-DCN-AGSAE-GPIA
   PDG-DOP-DCM-BOME-LALR
   PDG-DOP-DCM-BOME
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
   copubli-int-hors-europe
IF 9.598
TC 101
UR https://archimer.ifremer.fr/doc/2007/publication-3564.pdf
LA English
DT Article
DE ;Oyster innate immunity;Mollusk;Hemocyte;Epithelia;Antimicrobial
AB 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 LIPS, 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.
PY 2007
PD NOV
SO Proceedings of the National Academy of Sciences of the United States of America
SN 0027-8424
PU National Academy of Sciences
VL 104
IS 45
UT 000250897600040
BP 17759
EP 17764
DI 10.1073/pnas.0702281104
ID 3564
ER

EF