FN Archimer Export Format
PT J
TI First evidence of a potential antibacterial activity involving a laccase-type enzyme of the phenoloxidase system in Pacific oyster Crassostrea gigas haemocytes
BT 
AF LUNA-ACOSTA, Andrea
   SAULNIER, Denis
   POMMIER, Mylene
   HAFFNER, Philippe
   DE DECKER, Sophie
   RENAULT, Tristan
   THOMAS-GUYON, Helene
AS 1:1;2:2;3:1;4:2;5:2;6:2;7:1;
FF 1:;2:PDG-RBE-RMPF-EP;3:;4:PDG-RBE-AGSAE-LGP;5:PDG-DOP-DCOP-AQUAPOL;6:PDG-RBE-AGSAE-LGP;7:;
C1 Univ La Rochelle, CNRS, UMR 6250, Littoral Environm & Soc LIENSs, F-17402 La Rochelle 01, France.
   IFREMER, Lab Genet & Pathol (LGP), F-17390 La Tremblade, France.
C2 UNIV LA ROCHELLE, FRANCE
   IFREMER, FRANCE
SI TAHITI
   LA TREMBLADE
   UNIV-FRANCAISE
SE PDG-RBE-RMPF-EP
   PDG-RBE-AGSAE-LGP
   PDG-DOP-DCOP-AQUAPOL
   PDG-DOP-DCN-AGSAE-CRELA
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 3.322
TC 48
UR https://archimer.ifremer.fr/doc/00045/15598/13001.pdf
LA English
DT Article
DE ;Phenoloxidases;Antibacterial activity;Vibrio;Bivalve;Immunity
AB Phenoloxidases (POs) are a group of copper proteins including tyrosinase, catecholase and laccase. In several insects and crustaceans, antibacterial substances are produced through the PO cascade, participating in the direct killing of invading microorganisms. However, although POs are widely recognised as an integral part of the invertebrate immune defence system, experimental evidence is lacking that these properties are conserved in molluscs, and more particularly in the Pacific oyster Crassostrea gigas. In the present study, Vibrio splendidus LGP32 and Vibrio aestuarianus 02/041 growths were affected, after being treated with C. gigas haemocyte lysate supernatant (HLS), and either a common substrate of POs, l-3,4-dihydroxyphenylalanine (l-DOPA), to detect catecholase-type PO activity, or a specific substrate of laccase, p-phenylenediamine (PPD), to detect laccase-type PO activity. Interestingly, a higher bacterial growth inhibition was observed in the presence of PPD than in the presence of l-DOPA. These effects were suppressed when the specific PO inhibitor, phenylthiourea (PTU), was added to the medium. Results of the present study suggest, for the first time in a mollusc species, that antibacterial activities of HLS from C. gigas potentially involve POs, and more particularly laccase catalysed reactions.  Highlights  ► Bacterial growth inhibition was studied in two Vibrio oyster bacterial pathogens. ► Different Crassostrea gigas tissues, haemolymph fractions, and PO substrates, were tested. ► The inhibition occurred only in the presence of C. gigas HLS and PO substrates. ► Bacterial growth inhibition was suppressed with a PO inhibitor. ► Results suggest that HLS antibacterial activities involve laccase-type PO-catalysed reactions.
PY 2011
PD DEC
SO Fish & Shellfish Immunology
SN 1050-4648
PU Academic Press Ltd- Elsevier Science Ltd
VL 31
IS 6
UT 000298569700009
BP 795
EP 800
DI 10.1016/j.fsi.2011.07.016
ID 15598
ER

EF