FN Archimer Export Format
PT J
TI First description of French V. tubiashii strains pathogenic to mollusk: II. Characterization of properties of the proteolytic fraction of extracellular products
BT 
AF MERSNI ACHOUR, Rachida
   IMBERT-AUVRAY, Nathalie
   HUET, Valerie
   BEN CHEICK, Yosra
   FAURY, Nicole
   DOGHRI, Ibtissem
   ROUATBI, Sonia
   BORDENAVE, Stéphanie
   TRAVERS, Marie-Agnes
   SAULNIER, Denis
   FRUITIER-ARNAUDIN, Ingrid
AS 1:1,2,6;2:3;3:4;4:1;5:2;6:1;7:3;8:1;9:2;10:2,5;11:1,6;
FF 1:;2:;3:;4:;5:PDG-RBE-SG2M-LGPMM;6:;7:;8:;9:PDG-RBE-SG2M-LGPMM;10:PDG-RBE-RMPF;11:;
C1 UMR 7266 CNRS-Université de La Rochelle, LIENSs, Equipe Approches Moléculaires, Environnement-Santé, Avenue Michel Crépeau, 17000 La Rochelle, France
   Ifremer, SG2M-LGPMM, Laboratoire de Génétique et Pathologie des Mollusques Marins, Avenue de Mus de Loup, 17390 La Tremblade, France
   UMR 7266 CNRS-Université de La Rochelle, LIENSs, Equipe Animaux MARins à la variabilité Environnementale, 2 rue Olympe de Gouges, 17000 La Rochelle, France
   UMR 7266 CNRS-Université de La Rochelle, 2 rue Olympe de Gouges, 17000 La Rochelle, France
   Ifremer, Centre Ifremer du Pacifique, UMR 241 Ecosystèmes Insulaires Océaniens, Tahiti, 98719 Taravao, French Polynesia
   Fédération de Recherche en Environnement et Développement Durable, FR CNRS 3097, Université de La Rochelle, France
C2 CNRS, FRANCE
   IFREMER, FRANCE
   UNIV LA ROCHELLE, FRANCE
   UNIV LA ROCHELLE, FRANCE
   IFREMER, FRANCE
   UNIV LA ROCHELLE, FRANCE
SI LA TREMBLADE
   TAHITI
SE PDG-RBE-SG2M-LGPMM
   PDG-RBE-RMPF
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 2.11
TC 8
UR https://archimer.ifremer.fr/doc/00211/32203/30642.pdf
LA English
DT Article
DE ;ECPs;Oyster immune responses;Thermolysin-metalloprotease;Mass spectroscopy;ADAM substrate;Vibrio
AB Extracellular products (ECPs) of the French V. tubiashii strain 07/118 T2 were previously reported to be toxic for the Pacific oyster Crassostrea gigas. In this study we now assessed host cellular immune responses and bacterial potential effectors by which these ECPs can be associated with host damages. The adhesion capacity (28% inhibition) and phagocytosis ability (56% inhibition) of oyster hemocytes were the main functions affected following in vitro contact between hemocytes and V. tubiashii ECPs. This may be linked to the demonstration of the capability of ECPs to cleave various cellular substrates as oyster collagen. Moreover, a strong metalloproteolytic activity was recorded with general (azocasein) and specific (ADAM) substrates and characterized by the use of standard inhibitors and metal ions. The addition of 1, 10-phenanthroline and Zn2+ decreased proteolytic activity by about 80% and 50% respectively, confirming the presence of zinc metalloproteolytic activity in the ECPs. Mass spectrometry analyses of crude ECPs identified an extracellular zinc metalloprotease encoded by a gene with an open reading frame of 1821 bp (606 aa). Consensus zinc-binding motifs specific to thermolysin family and some glycosylation and phosphorylation sites were located on the deduced protein sequence. Even if taken together, our results let us wonder if this (these) zinc metalloprotease(s) could be involved in the impairment of hemocyte immunological functions, the direct implication of this (these) protein(s) in ECPs toxicity still has to be demonstrated.
PY 2014
PD NOV
SO Journal Of Invertebrate Pathology
SN 0022-2011
PU Academic Press Inc Elsevier Science
VL 123
UT 000344724600008
BP 49
EP 59
DI 10.1016/j.jip.2014.09.006
ID 32203
ER

EF