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A hemocyanin-derived antimicrobial peptide from the penaeid shrimp adopts an alpha-helical structure that specifically permeabilizes fungal membranes ArchiMer
Petit, Vanessa W.; Rolland, Jean-luc; Blond, Alain; Cazevieille, Chantal; Djediat, Chakib; Peduzzi, Jean; Goulard, Christophe; Bachere, Evelyne; Dupont, Joelle; Destoumieux-garzon, Delphine; Rebuffat, Sylvie.
Background. Hemocyanins are respiratory proteins with multiple functions. In diverse crustaceans hemocyanins can release histidine-rich antimicrobial peptides in response to microbial challenge. In penaeid shrimp, strictly antifungal peptides are released from the C-terminus of hemocyanins. Methods. The three-dimensional structure of the antifungal peptide PvHCt from Litopenaeus vannamei was determined by NMR. Its mechanism of action against the shrimp pathogen Fusarium oxysporum was investigated using immunochemistry, fluorescence and transmission electron microscopy. Results. PvHCt folded into an amphipathic α-helix in membrane-mimicking media and displayed a random conformation in aqueous environment. In contact with F. oxysporum, PvHCt bound...
Tipo: Text Palavras-chave: Antimicrobial peptide; Amphipathic helix; Fungi; Membrane bilayer; Nuclear magnetic resonance (NMR); Fluorescence microscopy.
Ano: 2016 URL: http://archimer.ifremer.fr/doc/00301/41202/40362.pdf
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