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| Registros recuperados: 56 | |
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| Escoubas, Jean-michel; Montagnani, Caroline; Le Roux, Frédérique; De Lorgeril, Julien; Berthe, Franck; Bachere, Evelyne. |
| We isolated complementary DNA (Cg-TIMP) from Crassostrea gigas that codes for a protein highly homologous to vertebrate tissue inhibitors of metalloproteinases (TIMPs). In vertebrates, TIMPs are multifunctional proteins that play a key role in extracellular matrix metabolism. They are involved in physiological processes (e.g. embryonic development, damage repair, angiogenesis) and pathological processes (e.g. inflammatory reactions, cancer). |
| Tipo: Text |
Palavras-chave: Proteine; Cg TIMP; ADN; Crassostrea gigas. |
| Ano: 2001 |
URL: http://archimer.ifremer.fr/doc/2001/acte-3268.pdf |
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| Pernet, Fabrice; Barret, Jean; Le Gall, Patrik; Malet, Nathalie; Pastoureaud, Annie; Munaron, Dominique; De Lorgeril, Julien; Bachere, Evelyne; Vaquer, Andre; Huvet, Arnaud; Corporeau, Charlotte; Normand, Julien; Boudry, Pierre; Moal, Jeanne; Quere, Claudie; Quilien, Virgile; Daniel, Jean-yves; Pepin, Jean-francois; Saulnier, Denis; Gonzalez, Jean-louis. |
| This study was conducted in the Mediterranean area during a mass mortality event of Pacific oyster Crassostrea gigas. The objectives of this work were to increase our understanding of the mass mortality phenomena in Pacific oysters, to identify risky cultivation practises and to propose mitigation strategies. In the first part of this work, we followed environmental parameters of the Thau lagoon in relation with mortality events. Then, we compared mortality and growth parameters of oysters as a function of their origins, their development stages and cultivation sites in relation with energetic, reproduction and pathogens. Finally, we conducted transfer experiments where oysters maintained free of mortality in open sea were transferred in the Thau lagoon... |
| Tipo: Text |
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| Ano: 2010 |
URL: http://archimer.ifremer.fr/doc/00002/11354/7927.pdf |
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| Cochennec-laureau, Nathalie; Baud, Jean-pierre; Pepin, Jean-francois; Benabdelmouna, Abdellah; Soletchnik, Patrick; Lupo, Coralie; Garcia, Celine; Arzul, Isabelle; Boudry, Pierre; Huvet, Arnaud; Pernet, Fabrice; Bachere, Evelyne; Bedier, Edouard; Petton, Bruno; Gaussem, Florian; Stanisiere, Jean-yves; Degremont, Lionel. |
| Depuis 2008, la filière ostréicole française doit faire face à des surmortalités exceptionnelles des naissains d’huîtres creuses, Crassostrea gigas, (huîtres de moins d’un an) comprises entre 60 et 90% dans tous les sites d’élevage. Des cas de mortalité similaires ont été décrits en Irlande, dans les îles anglo-normandes, au Portugal en 2009 et au Royaume-Uni en 2010. Récemment deux épisodes de mortalité, associés à la présence d’un virus OsHV1 μvar (ou un variant très proche) ont été également décrits en Nouvelle Zélande (décembre 2010) et en Australie (janvier 2011) soulignant la vulnérabilité de la filière ostréicole dans le monde. L’objectif de ce document est de faire un point sur les recherches menées depuis l’apparition de ce phénomène et de... |
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| Ano: 2011 |
URL: http://archimer.ifremer.fr/doc/00033/14423/11719.pdf |
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| Destoumieux, Delphine; Bulet, Philippe; Loew, Damarys; Van Dorsselaer, Alain; Rodriguez, Jenny; Bachere, Evelyne. |
| We report here the isolation of three members of a new family of antimicrobial peptides from the hemolymph of shrimps Penaeus vannamei in which immune response has not been experimentally induced. The three molecules display antimicrobial activity against fungi and bacteria with a predominant activity against Gram-positive bacteria. The complete sequences of these peptides were determined by a combination of enzymatic cleavages, Edman degradation, mass spectrometry, and cDNA cloning using a hemocyte cDNA library. The mature molecules (50 and 62 residues) are characterized by an NH2-terminal domain rich in proline residues and a COOH-terminal domain containing three intramolecular disulfide bridges. One of these molecules is post-translationally modified by... |
| Tipo: Text |
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| Ano: 1997 |
URL: http://archimer.ifremer.fr/doc/00335/44649/57344.pdf |
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| Rolland, Jean-luc; Abdelouahab, Mahdia; Dupont, J.; Lefevre, F.; Bachere, Evelyne; Romestand, Bernard. |
| The present study reports the characterization of Ls-Stylicin1, a novel antimicrobial peptide from the penaeid shrimp, Litopenoeus stylirostris. The predicted mature peptide of 82 residues is negatively charged (theoretical pl=5.0) and characterized by a proline-rich N-terminal region and a C-terminal region containing 13 cysteine residues. The recombinant Ls-Stylicin1 has been isolated in both monomeric and dimeric forms. Both display strong antifungal activity against Fusarium oxysporum (1.25 mu M < MIC <2.5 mu M), a pathogenic fungus of shrimp, but lower antimicrobial activity against Gram () bacteria, Vibrio sp. (40 mu M < MIC <80 mu M). However, rLs-Stylicin1 is able to agglutinate Vibrio pennaeicidae in vitro in agreement with its potent... |
| Tipo: Text |
Palavras-chave: Ls-Stylicin 1; Peptide; Shrimp; Antifungal; Agglutination; Vibrio. |
| Ano: 2010 |
URL: http://archimer.ifremer.fr/doc/00003/11387/8094.pdf |
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| 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 |
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| Ano: 2010 |
URL: http://archimer.ifremer.fr/doc/00003/11421/8044.pdf |
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| 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 |
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| 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 |
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| Bachere, Evelyne; Grizel, Henri. |
| A new Haplosporidie has been observed in the flat oyster Ostrea edulis from the Mediterranean Sea. Different development stages have been described in light and electron microscopy. The characteristics of the spores and especially the presence of at least four sporal filaments enable us to distinguish this Haplosporidie from those already described in the Atlantic flat oysters. Different haplosporidies have been described in the oyster. Some are known as being pathogenic, Minchinia costalis (Andrews et al., 1962 and 1978; Couch 1967) and Minchinia nelsoni (Haskin et al., 1966; Farley 1968 and 1975), others, identified only recently, are considered as occasional parasites (Van Banning, 1977). During the research conducted on Bonamia ostreae (Pichot et al.,... |
| Tipo: Text |
Palavras-chave: Pathologie; Haplosporidium; Parasite; Ostrea edulis; Huître plate. |
| Ano: 1982 |
URL: http://archimer.ifremer.fr/doc/1982/publication-6576.PDF |
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| 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 |
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| Ano: 2013 |
URL: http://archimer.ifremer.fr/doc/00160/27077/25236.pdf |
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| Gueguen, Yannick; Garnier, Julien; Robert, Lorenne; Lefranc, Marie-paule; Mougenot, Isabelle; De Lorgeril, Julien; Janech, Michael; Gross, Paul S.; Warr, Gregory W.; Cuthbertson, Brandon; Barracco, Margherita A.; Bulet, Philippe; Aumelas, André; Yang, Yinshan; Bo, Dong; Xiang, Jianhai; Tassanakajon, Anchalee; Piquemal, Piquemal; Bachere, Evelyne. |
| Antimicrobial peptides play a major role in innate immunity. The penaeidins, initially characterized from the shrimp Litopenaeus vannamei, are a family of antimicrobial peptides that appear to be expressed in all penaeid shrimps. As of recent, a large number of penaeid nucleotide sequences have been identified from a variety of penaeid shrimp species and these sequences currently reside in several databases under unique identifiers with no nomenclatural continuity. To facilitate research in this field and avoid potential confusion due to a diverse number of nomenclatural designations, we have made a systematic effort to collect, analyse, and classify all the penaeidin sequences available in every database. We have identified a common penaeidin signature... |
| Tipo: Text |
Palavras-chave: Nomenclature; Sequence database; Crustacea; Antimicrobial peptide; Penaeid shrimp; Penaeidin. |
| Ano: 2006 |
URL: http://archimer.ifremer.fr/doc/2006/publication-2332.pdf |
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| Destoumieux, Delphine; Munoz, Marcello; Cosseau, Céline; Rodriguez, Jenny; Bulet, Philippe; Comps, Marie-annick; Bachere, Evelyne. |
| Penaeidins are members of a new family of antimicrobial peptides isolated from a crustacean, which present both Gram-positive antibacterial and antifungal activities. We have studied the localization of synthesis and storage of penaeidins in the shrimp Penaeus vannamei. The distribution of penaeidin transcripts and peptides in various tissues reveals that penaeidins are constitutively synthesized and stored in the shrimp haemocytes. It was shown by immunocytochemistry, at both optical and ultrastructural levels, that the peptides are localized in granulocyte cytoplasmic granules, The expression and localization of penaeidins were further analysed in shrimp subjected to microbial challenge. We found that (1) penaeidin mRNA levels decrease in circulating... |
| Tipo: Text |
Palavras-chave: Crustacean immunity; Penaeid shrimp; Haemocyte; Chitin binding; Antimicrobial peptide. |
| Ano: 2000 |
URL: http://archimer.ifremer.fr/doc/2000/publication-412.pdf |
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| Registros recuperados: 56 | |
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