FN Archimer Export Format
PT J
TI Functional Insights From the Evolutionary Diversification of Big Defensins
BT 
AF GERDOL, Marco
   SCHMITT, Paulina
   VENIER, Paola
   ROCHA, Gustavo
   ROSA, Rafael Diego
   DESTOUMIEUX-GARZON, Delphine
AS 1:1;2:2;3:3;4:4;5:4;6:5;
FF 1:;2:;3:;4:;5:;6:;
C1 Univ Trieste, Dept Life Sci, Trieste, Italy.
   Pontificia Univ Catolica Valparaiso, Inst Biol, Lab Genet & Inmunol Mol, Valparaiso, Chile.
   Univ Padua, Dept Biol, Padua, Italy.
   Univ Fed Santa Catarina, Dept Cell Biol Embryol & Genet, Lab Immunol Appl Aquaculture, Florianopolis, SC, Brazil.
   Univ Perpignan, Univ Montpellier, CNRS, IHPE, Via Domitia, Montpellier, France.
C2 UNIV TRIESTE, ITALY
   UNIV PONTIFICIA CATOLICA VALPARAISO, CHILE
   UNIV PADUA, ITALY
   UNIV FED SANTA CATARINA, BRAZIL
   UNIV PERPIGNAN, FRANCE
UM IHPE
IN WOS Cotutelle UMR
   DOAJ
   copubli-europe
   copubli-int-hors-europe
   copubli-sud
IF 7.561
TC 32
UR https://archimer.ifremer.fr/doc/00695/80739/84019.pdf
   https://archimer.ifremer.fr/doc/00695/80739/84020.docx
   https://archimer.ifremer.fr/doc/00695/80739/84021.docx
   https://archimer.ifremer.fr/doc/00695/80739/84022.xlsx
LA English
DT Article
DE ;antimicrobial peptide;defensin;evolution;nanonet;host defense (antimicrobial) peptides
AB Big defensins are antimicrobial polypeptides believed to be the ancestors of beta-defensins, the most evolutionary conserved family of host defense peptides (HDPs) in vertebrates. Nevertheless, big defensins underwent several independent gene loss events during animal evolution, being only retained in a limited number of phylogenetically distant invertebrates. Here, we explore the evolutionary history of this fascinating HDP family and investigate its patchy distribution in extant metazoans. We highlight the presence of big defensins in various classes of lophotrochozoans, as well as in a few arthropods and basal chordates (amphioxus), mostly adapted to life in marine environments. Bivalve mollusks often display an expanded repertoire of big defensin sequences, which appear to be the product of independent lineage-specific gene tandem duplications, followed by a rapid molecular diversification of newly acquired gene copies. This ongoing evolutionary process could underpin the simultaneous presence of canonical big defensins and non-canonical (beta-defensin-like) sequences in some species. The big defensin genes of mussels and oysters, two species target of in-depth studies, are subjected to gene presence/absence variation (PAV), i.e., they can be present or absent in the genomes of different individuals. Moreover, big defensins follow different patterns of gene expression within a given species and respond differently to microbial challenges, suggesting functional divergence. Consistently, current structural data show that big defensin sequence diversity affects the 3D structure and biophysical properties of these polypeptides. We discuss here the role of the N-terminal hydrophobic domain, lost during evolution toward beta-defensins, in the big defensin stability to high salt concentrations and its mechanism of action. Finally, we discuss the potential of big defensins as markers for animal health and for the nature-based design of novel therapeutics active at high salt concentrations.
PY 2020
PD APR
SO Frontiers In Immunology
SN 1664-3224
PU Frontiers Media Sa
VL 11
IS 758
UT 000535551600001
DI 10.3389/fimmu.2020.00758
ID 80739
ER

EF