FN Archimer Export Format PT J TI Vibrio aestuarianus zinc metalloprotease causes lethality in the Pacific oyster Crassostrea gigas and impairs the host cellular immune defenses BT AF LABREUCHE, Yannick LE ROUX, Frederique HENRY, Joel ZATYLNY, Celine HUVET, Arnaud LAMBERT, Christophe SOUDANT, Philippe MAZEL, Didier NICOLAS, Jean-Louis AS 1:1,2;2:3,4,5;3:6;4:6;5:2;6:7;7:7;8:3,4;9:2; FF 1:PDG-DOP-DCOP-LEADNC-LAC;2:PDG-DOP-DCB-PFOM;3:;4:;5:PDG-DOP-DCB-PFOM-PI;6:;7:;8:;9:PDG-DOP-DCB-PFOM-PI; C1 IFREMER, Dept Lagons Ecosyst & Aquaculture Durable Nouvell, Stn St Vincent, Noumea 98846, New Caledonia. IFREMER Physiol & Ecophysiol Mollusques Marins, Ctr Brest, UMR 100, F-29280 Plouzane, France. Inst Pasteur, Unite Plast Genome Bacterien, Dept Genomes & Genet, F-75015 Paris, France. CNRS, URA 2171, F-75015 Paris, France. IFREMER, Lab Genet & Pathol, F-17390 La Tremblade, France. Univ Caen Basse Normandie, IFREMER Physiol & Ecophysiol Mollusques Marins, Lab Biol & Biotechnol Marines, UMR 100, F-14032 Caen, France. Univ Bretagne Occidentale, Inst Univ Europeen Mer, Lab Sci Environm Marin, F-29280 Plouzane, France. C2 IFREMER, FRANCE IFREMER, FRANCE INST PASTEUR, FRANCE CNRS, FRANCE IFREMER, FRANCE UNIV CAEN, FRANCE UBO, FRANCE SI SAINT VINCENT BREST SE PDG-DOP-DCOP-LEADNC-LAC PDG-DOP-DCB-PFOM PDG-DOP-DCB-PFOM-PI IN WOS Ifremer jusqu'en 2018 copubli-france copubli-univ-france IF 3.044 TC 59 UR https://archimer.ifremer.fr/doc/00015/12649/9588.pdf LA English DT Article DE ;Vibrio aestuarianus;Metalloprotease;Crassostrea gigas;Oyster;Hemocytes;Extracellular products AB Extracellular products (ECPs) of the pathogenic Vibrio aestuarianus 01/32 were previously reported to display lethality in Crassostrea gigas oysters and to cause morphological changes and immunosuppression in oyster hemocytes. To identify the source of this toxicity, biochemical and genetic approaches were developed. ECP protease activity and lethality were shown to be significantly reduced following incubation with metal chelators, suggesting the involvement of a zinc metalloprotease. An open reading frame of 1836 bp encoding a 611-aa metalloprotease (designated yam) was identified. The deduced protein sequence showed high homology to other Vibrio metalloproteases reported to be involved in pathogenicity. To further confirm the role of this enzyme in ECP toxicity, a plasmid carrying the yarn gene under the control of an araC-P-BAD expression cassette was transferred to a Vibrio splendidus related strain, LMC20012(T), previously characterized as non-pathogenic to oysters. Expression of Vam conferred a toxic phenotype to LMG20012(T) ECPs in vivo and cytotoxicity to oyster hemocytes in vitro. Collectively, these data suggest that the Vam metalloprotease is a major contributor to the toxicity induced by V aestuarianus ECPs and is involved in the impairment of oyster hemocyte functions. (C) 2010 Elsevier Ltd. All rights reserved. PY 2010 PD NOV SO Fish & Shellfish Immunology SN 1050-4648 PU Academic Press Ltd- Elsevier Science Ltd VL 29 IS 5 UT 000282470400007 BP 753 EP 758 DI 10.1016/j.fsi.2010.07.007 ID 12649 ER EF