Consulta: creatorFacets:"Barreto, Cairé"
Registros recuperados: 2
Data/hora: 09/06/2024 15:32:17

The Ancestral N-Terminal Domain of Big Defensins Drives Bacterially Triggered Assembly into Antimicrobial Nanonets
Provedor de dados: 5
Autores: Loth, Karine; Vergnes, Agnes; Barreto, Cairé; Voisin, Sébastien N; Meudal, Hervé; Da Silva, Jennifer; Bressan, Albert; Belmadi, Nawal; Bachère, Evelyne; Aucagne, Vincent; Cazevielle, Chantal; Marchandin, Hélène; Rosa, Rafael Diego; Bulet, Philippe; Touqui, Lhousseine; Delmas, Agnès F.; Destoumieux-garzón, Delphine.
Big defensins, ancestors of β-defensins, are composed of a β-defensin-like C-terminal domain and a globular hydrophobic ancestral N-terminal domain. This unique structure is found in a limited number of phylogenetically distant species, including mollusks, ancestral chelicerates, and early-branching cephalochordates, mostly living in marine environments. One puzzling evolutionary issue concerns the advantage for these species of having maintained a hydrophobic domain lost during evolution toward β-defensins. Using native ligation chemistry, we produced the oyster Crassostrea gigas BigDef1 (Cg-BigDef1) and its separate domains. Cg-BigDef1 showed salt-stable and broad-range bactericidal activity, including against multidrug-resistant human clinical isolates...
Tipo: Text
Palavras-chave: MRSA; Antimicrobial peptides; Antimicrobial resistance; Defensins; Fibrils; Innate immunity; Mechanisms of action; Nuclear magnetic resonance.
Ano: 2019
URL: https://archimer.ifremer.fr/doc/00588/70057/68000.pdf

Litopenaeus vannamei stylicins are constitutively produced by hemocytes and intestinal cells and are differentially modulated upon infections
Provedor de dados: 5
Autores: Farias, Natanael Dantas; Falchetti, Marcelo; Matos, Gabriel Machado; Schmitt, Paulina; Barreto, Cairé; Argenta, Nicolas; Rolland, Jean-luc; Bachère, Evelyne; Perazzolo, Luciane Maria; Rosa, Rafael Diego.
Stylicins are anionic antimicrobial host defense peptides (AAMPs) composed of a proline-rich N-terminal region and a C-terminal portion containing 13 conserved cysteine residues. Here, we have increased our knowledge about these unexplored crustacean AAMPs by the characterization of novel stylicin members in the most cultivated penaeid shrimp, Litopenaeus vannamei. We showed that the L. vannamei stylicin family is composed of two members (Lvan-Stylicin1 and Lvan-Stylicin2) encoded by different loci which vary in gene copy number. Unlike the other three gene-encoded antimicrobial peptide families from penaeid shrimp, the expression of Lvan-Stylicins is not restricted to hemocytes. Indeed, they are also produced by the columnar epithelial cells lining the...
Tipo: Text
Palavras-chave: Crustacean; Penaeid shrimp; Invertebrate immunity; Antimicrobial peptide; Host defense peptide; Molecular diversity.
Ano: 2019
URL: https://archimer.ifremer.fr/doc/00466/57816/60102.pdf