FN Archimer Export Format
PT J
TI New Insights Into Biomphalysin Gene Family Diversification in the Vector Snail Biomphalaria glabrata
BT 
AF Pinaud, Silvain
   Tetreau, Guillaume
   Poteaux, Pierre
   Galinier, Richard
   Chaparro, Cristian
   Lassalle, Damien
   Portet, Anaïs
   Simphor, Elodie
   Gourbal, Benjamin
   Duval, David
AS 1:1,2;2:1,2;3:1,2;4:1,2;5:1,2;6:1,2;7:1,2;8:1,2;9:1,2;10:1,2;
FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:;
C1 IHPE, Univ Montpellier, CNRS, IFREMER, Univ Perpignan Via Domitia, Perpignan, France
   CNRS, IFREMER, University of Montpellier, Perpignan, France
C2 UNIV MONTPELLIER, FRANCE
   CNRS, FRANCE
UM IHPE
IN WOS Cotutelle UMR
   DOAJ
IF 8.787
TC 12
UR https://archimer.ifremer.fr/doc/00687/79909/82814.pdf
   https://archimer.ifremer.fr/doc/00687/79909/82815.pdf
   https://archimer.ifremer.fr/doc/00687/79909/82816.pdf
   https://archimer.ifremer.fr/doc/00687/79909/82817.pdf
   https://archimer.ifremer.fr/doc/00687/79909/82818.tif
LA English
DT Article
DE ;biomphalaria;biomphalysin;aerolysin;invertebrate immunity;pore-forming toxin (PFT);structure
AB Aerolysins initially characterized as virulence factors in bacteria are increasingly found in massive genome and transcriptome sequencing data from metazoans. Horizontal gene transfer has been demonstrated as the main way of aerolysin-related toxins acquisition in metazoans. However, only few studies have focused on their potential biological functions in such organisms. Herein, we present an extensive characterization of a multigene family encoding aerolysins - named biomphalysin - in Biomphalaria glabrata snail, the intermediate host of the trematode Schistosoma mansoni. Our results highlight that duplication and domestication of an acquired bacterial toxin gene in the snail genome result in the acquisition of a novel and diversified toxin family. Twenty-three biomphalysin genes were identified. All are expressed and exhibited a tissue-specific expression pattern. An in silico structural analysis was performed to highlight the central role played by two distinct domains i) a large lobe involved in the lytic function of these snail toxins which constrained their evolution and ii) a small lobe which is structurally variable between biomphalysin toxins and that matched to various functional domains involved in moiety recognition of targets cells. A functional approach suggests that the repertoire of biomphalysins that bind to pathogens, depends on the type of pathogen encountered. These results underline a neo-and sub-functionalization of the biomphalysin toxins, which have the potential to increase the range of effectors in the snail’s immune arsenal. 
PY 2021
PD APR
SO Frontiers In Immunology
SN 1664-3224
PU Frontiers Media SA
VL 12
UT 000640354500001
DI 10.3389/fimmu.2021.635131
ID 79909
ER

EF