|
|
| 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 |
| |
