Consulta: creatorFacets:"Saune, Laure"
Registros recuperados: 2
Data/hora: 06/06/2024 10:49:48

Evidence of a bactericidal permeability increasing protein in an invertebrate, the Crassostrea gigas Cg-BPI
Provedor de dados: 5
Autores: 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.
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,...
Tipo: Text
Palavras-chave: Oyster innate immunity; Mollusk; Hemocyte; Epithelia; Antimicrobial.
Ano: 2007
URL: http://archimer.ifremer.fr/doc/2007/publication-3564.pdf

Functional Divergence in Shrimp Anti-Lipopolysaccharide Factors (ALFs): From Recognition of Cell Wall Components to Antimicrobial Activity
Provedor de dados: 5
Autores: Rosa, Rafael Diego; Vergnes, Agnes; De Lorgeril, Julien; Goncalves, Priscila; Perazzolo, Luciane Maria; Saune, Laure; Romestand, Bernard; Fievet, Julie; Gueguen, Yannick; Bachere, Evelyne; Destoumieux-garzon, Delphine.
Antilipopolysaccharide factors (ALFs) have been described as highly cationic polypeptides with a broad spectrum of potent antimicrobial activities. In addition, ALFs have been shown to recognize LPS, a major component of the Gram-negative bacteria cell wall, through conserved amino acid residues exposed in the four-stranded beta-sheet of their three dimensional structure. In penaeid shrimp, ALFs form a diverse family of antimicrobial peptides composed by three main variants, classified as ALF Groups A to C. Here, we identified a novel group of ALFs in shrimp (Group D ALFs), which corresponds to anionic polypeptides in which many residues of the LPS binding site are lacking. Both Group B (cationic) and Group D (anionic) shrimp ALFs were produced in a...
Tipo: Text
Ano: 2013
URL: http://archimer.ifremer.fr/doc/00160/27077/25236.pdf