FN Archimer Export Format
PT J
TI Nigritoxin is a bacterial toxin for crustaceans and insects
BT 
AF LABREUCHE, Yannick
   CHENIVESSE, Sabine
   JEUDY, Alexandra
   LE PANSE, Sophie
   BOULO, Viviane
   ANSQUER, Dominique
   PAGES, Sylvie
   GIVAUDAN, Alain
   CZJZEK, Mirjam
   LE ROUX, Frederique
AS 1:1,2;2:2;3:2;4:3;5:4;6:4;7:5;8:5;9:2;10:1,2;
FF 1:PDG-RBE-PFOM;2:;3:;4:;5:PDG-RBE-LEADNC;6:PDG-RBE-LEADNC;7:;8:;9:;10:PDG-RBE-PFOM;
C1 IFREMER, Unite Physiol Fonct Organismes Marins, ZI Pointe Diable, CS 10070, F-29280 Plouzane, France.
   UPMC Paris 06, CNRS, Sorbonne Univ, UMR 8227,Integrat Biol Marine Models,Stn Biol Ros, CS 90074, F-29688 Roscoff, France.
   CNRS, Stn Biol Roscoff, FR 2424,Pl Georges Teissier,CS 90074, F-29688 Roscoff, France.
   IFREMER, Dept Lagons Ecosyst & Aquaculture Durables Nouvel, BP 2059, Noumea 98846, New Caledonia.
   Univ Montpellier 2, UMR Diversite Genomes & Interact Microorganismes, 2 Pl Eugene Bataillon, F-34095 Montpellier 5, France.
C2 IFREMER, FRANCE
   UNIV PARIS 06, FRANCE
   CNRS, FRANCE
   IFREMER, FRANCE
   UNIV MONTPELLIER, FRANCE
SI ROSCOFF
   SAINT VINCENT
SE PDG-RBE-PFOM
   PDG-RBE-LEADNC
IN WOS Ifremer jusqu'en 2018
   DOAJ
   copubli-france
   copubli-univ-france
IF 12.353
TC 7
UR https://archimer.ifremer.fr/doc/00408/51934/52563.pdf
   https://archimer.ifremer.fr/doc/00408/51934/52564.pdf
   https://archimer.ifremer.fr/doc/00408/51934/52565.pdf
LA English
DT Article
AB The Tetraconata (Pancrustacea) concept proposes that insects are more closely related to aquatic crustaceans than to terrestrial centipedes or millipedes. The question therefore arises whether insects have kept crustacean-specific genetic traits that could be targeted by specific toxins. Here we show that a toxin (nigritoxin), originally identified in a bacterial pathogen of shrimp, is lethal for organisms within the Tetraconata and non-toxic to other animals. X-ray crystallography reveals that nigritoxin possesses a new protein fold of the α/β type. The nigritoxin N-terminal domain is essential for cellular translocation and likely encodes specificity for Tetraconata. Once internalized by eukaryotic cells, nigritoxin induces apoptotic cell death through structural features that are localized in the C-terminal domain of the protein. We propose that nigritoxin will be an effective means to identify a Tetraconata evolutionarily conserved pathway and speculate that nigritoxin holds promise as an insecticidal protein. 
PY 2017
PD NOV
SO Nature Communications
SN 2041-1723
PU Nature Publishing Group
VL 8
IS 1
UT 000414229000012
DI 10.1038/s41467-017-01445-z
ID 51934
ER

EF