Consulta: creatorFacets:"Destoumieux Garzon, Delphine"
Registros recuperados: 6
Data/hora: 06/06/2024 08:11:38

The Pacific Oyster Mortality Syndrome, a Polymicrobial and Multifactorial Disease: State of Knowledge and Future Directions
Provedor de dados: 5
Autores: Petton, Bruno; Destoumieux Garzon, Delphine; Pernet, Fabrice; Toulza, Eve; De Lorgeril, Julien; Degremont, Lionel; Mitta, Guillaume.
The Pacific oyster (Crassostreae gigas) has been introduced from Asia to numerous countries around the world during the 20th century. C. gigas is the main oyster species farmed worldwide and represents more than 98% of oyster production. The severity of disease outbreaks that affect C. gigas, which primarily impact juvenile oysters, has increased dramatically since 2008. The most prevalent disease, Pacific oyster mortality syndrome (POMS), has become panzootic and represents a threat to the oyster industry. Recently, major steps towards understanding POMS have been achieved through integrative molecular approaches. These studies demonstrated that infection by Ostreid herpesvirus type 1 µVar (OsHV-1 µvar) is the first critical step in the infectious process...
Tipo: Text
Palavras-chave: Pacific oyster mortality syndrome; Polymicrobial disease; Multifactorial disease; Crassostrea gigas; OsHV-1; Opportunistic bacterial pathogens.
Ano: 2021
URL: https://archimer.ifremer.fr/doc/00679/79158/81669.pdf

Oyster hemocytes express a proline-rich peptide displaying synergistic antimicrobial activity with a defensin
Provedor de dados: 5
Autores: Gueguen, Yannick; Romestand, Bernard; Fievet, Julie; Schmitt, Paulina; Destoumieux Garzon, Delphine; Franck, Vandenbulcke; Philippe, Bulet; Bachere, Evelyne.
A cDNA sequence that encodes a 61-amino acid polypeptide precursor with homologies to proline-rich antimicrobial peptides (AMPs) was identified in the oyster Crassostrea gigas. After release of a hydrophobic signal peptide. the resulting 37-amino acid peptide, Cg-Prp, is composed of an acidic region and a cationic proline-rich region. To evaluate the biological properties of Cg-Prp, multiple proline-rich peptides corresponding to putative processing of the full-length Cg-Prp were synthesized. A limited antimicrobial activity was observed for two of them, which also showed strong synergistic antimicrobial activity with Cg-Def, a defensin from C gigas. To our knowledge, this is the first evidence of synergy between a defensin and another AMP in an...
Tipo: Text
Palavras-chave: Antimicrobial peptide; Mollusk; Synergy; Invertebrate; Innate immunity; Pacific oyster.
Ano: 2009
URL: http://archimer.ifremer.fr/doc/2009/publication-6232.pdf

The major outer membrane protein OmpU of Vibrio splendidus contributes to host antimicrobial peptide resistance and is required for virulence in the oyster Crassostrea gigas
Provedor de dados: 5
Autores: Duperthuy, Marylise; Binesse, Johan; Le Roux, Frederique; Romestand, Bernard; Caro, Audrey; Got, Patrice; Givaudan, Alain; Mazel, Didier; Bachere, Evelyne; Destoumieux Garzon, Delphine.
Vibrio splendidus, strain LGP32, is an oyster pathogen associated with the summer mortalities affecting the production of Crassostrea gigas oysters worldwide. Vibrio splendidus LGP32 was shown to resist to up to 10 mu M Cg-Def defensin and Cg-BPI bactericidal permeability increasing protein, two antimicrobial peptides/proteins (AMPs) involved in C. gigas immunity. The resistance to both oyster Cg-Def and Cg-BPI and standard AMPs (polymyxin B, protegrin, human BPI) was dependent on the ompU gene. Indeed, upon ompU inactivation, minimal bactericidal concentrations decreased by up to fourfold. AMP resistance was restored upon ectopic expression of ompU. The susceptibility of bacterial membranes to AMP-induced damages was independent of the ompU-mediated AMP...
Tipo: Text
Ano: 2010
URL: http://archimer.ifremer.fr/doc/00003/11421/8044.pdf

NMR Structure of rALF-Pm3, an Anti-Lipopolysaccharide Factor from Shrimp: Model of the Possible Lipid A-Binding Site
Provedor de dados: 5
Autores: Yang, Yinshan; Boze, Helene; Chemardin, Patrick; Padilla, Andre; Moulin, Guy; Tassanakajon, Anchalee; Pugniere, Martine; Roquet, Francoise; Destoumieux Garzon, Delphine; Gueguen, Yannick; Bachere, Evelyne; Aumelas, Andre.
The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which...
Tipo: Text
Palavras-chave: Ultracentrifugation; Surface plasmon resonance; Septic shock; Structure; NMR; Lipid A; Lipopolysaccharide; Anti lipopolysaccharide factor.
Ano: 2009
URL: http://archimer.ifremer.fr/doc/2009/publication-6320.pdf

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

Massive Gene Expansion and Sequence Diversification Is Associated with Diverse Tissue Distribution, Regulation and Antimicrobial Properties of Anti-Lipopolysaccharide Factors in Shrimp
Provedor de dados: 5
Autores: Matos, Gabriel Machado; Schmitt, Paulina; Barreto, Caire; Farias, Natanael Dantas; Toledo-silva, Guilherme; Guzman, Fanny; Destoumieux Garzon, Delphine; Perazzolo, Luciane Maria; Rosa, Rafael Diego.
Anti-lipopolysaccharide factors (ALFs) are antimicrobial peptides with a central β-hairpin structure able to bind to microbial components. Mining sequence databases for ALFs allowed us to show the remarkable diversity of ALF sequences in shrimp. We found at least seven members of the ALF family (Groups A to G), including two novel Groups (F and G), all of which are encoded by different loci with conserved gene organization. Phylogenetic analyses revealed that gene expansion and subsequent diversification of the ALF family occurred in crustaceans before shrimp speciation occurred. The transcriptional profile of ALFs was compared in terms of tissue distribution, response to two pathogens and during shrimp development in Litopenaeus vannamei, the most...
Tipo: Text
Palavras-chave: Host defense peptide; Antimicrobial peptide; Anti-LPS factor; Hostmicrobe relationship; Functional diversity; Invertebrate immunity; Crustacean; Antimicrobial activity.
Ano: 2018
URL: https://archimer.ifremer.fr/doc/00464/57523/59711.pdf