Consulta: subjectFacets:"Mollusc bivalve"
Registros recuperados: 2
Data/hora: 06/06/2024 10:27:32

Molecular characterization of two isoforms of defensin from hemocytes of the oyster Crassostrea gigas
Provedor de dados: 5
Autores: Gonzalez, Marcelo; Gueguen, Yannick; Desserre, Geraldine; De Lorgeril, Julien; Romestand, Bernard; Bachere, Evelyne.
Antimicrobial peptides (AMPs) are important components of the host innate immune response against microbial invasion. We previously characterized the first AMP from an oyster, a defensin, that was shown to be continuously expressed in the mantle of Crassostrea gigas. In this study, we report the cDNA cloning of two new isoforms of the defensin AMP family (Cg-defh1 and Cg-defh2) from the hemocytes of the oyster. The deduced amino acid sequences reveal two peptides of 73 amino acid residues with a mature portion consisting of 43 amino acid residues. Cy-Defh1 and CyDefh2 share 86% amino acid identity and belong to the "arthropod-molluscs defensin family". qRT-PCR analyses indicate that Cg-defh2 is continuously expressed in the hemocytes of C. gigas. In...
Tipo: Text
Palavras-chave: Defensin; Antimicrobial peptide; Hemocytes; Pacific oyster; Marine invertebrate; Mollusc bivalve.
Ano: 2007
URL: http://archimer.ifremer.fr/doc/2007/publication-2331.pdf

Evidence in oyster of a plasma extracellular superoxide dismutase which binds LPS
Provedor de dados: 5
Autores: Gonzalez, Marcelo; Romestand, Bernard; Fievet, Julie; Huvet, Arnaud; Lebart, M; Gueguen, Yannick; Bachere, Evelyne.
We have characterized in the oyster Crassostrea gigas an extracellular superoxide dismutase (Cg-EcSOD) which appears to bind lipopolysaccharides (LPS). The protein has been purified from the oyster plasma and identified as a Cu/ZnSOD according to its N-terminal sequencing and biological activity. Cg-EcSOD expression and synthesis are restricted to hemocytes as revealed by in situ hybridization and immunocytochemistry. Cg-EcSOD-expressing hemocytes were seen in blood circulation, in connective tissues, and closely associated to endothelium blood vessels. Cg-EcSOD presents in its amino acid sequence a LPS-binding motif found in the endotoxin receptor CD14 and we show that the protein displays an affinity to Escherichia coli bacteria and with LPS and Lipid A....
Tipo: Text
Palavras-chave: Beta integrin; Oxidative burst; Hemocyte; Crassostrea gigas; Invertebrate; Mollusc bivalve.
Ano: 2005
URL: http://archimer.ifremer.fr/doc/2005/publication-3583.pdf