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...
Published in: | Proceedings of the National Academy of Sciences |
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Main Authors: | , , , , , , , , , , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
HAL CCSD
2007
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Subjects: | |
Online Access: | https://hal.archives-ouvertes.fr/hal-03828696 https://doi.org/10.1073/pnas.0702281104 |
Summary: | 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. |
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