FN Archimer Export Format
PT J
TI Worms’ Antimicrobial Peptides
BT 
AF Bruno, Renato
   Maresca, Marc
   Canaan, Stéphane
   Cavalier, Jean-François
   Mabrouk, Kamel
   Boidin-Wichlacz, Céline
   Olleik, Hamza
   ZEPPILLI, Daniela
   Brodin, Priscille
   Massol, François
   Jollivet, Didier
   Jung, Sasha
   Tasiemski, Aurélie
AS 1:1,2;2:3;3:4;4:4;5:5;6:1,2;7:3;8:6;9:1;10:1,2;11:7;12:8;13:1,2;
FF 1:;2:;3:;4:;5:;6:;7:;8:PDG-REM-EEP-LEP;9:;10:;11:;12:;13:;
C1 Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 – UMR 8204 - CIIL - Center for Infection and Immunity of Lille, F-59000 Lille, France
   Univ. Lille, CNRS, UMR 8198 - Evo-Eco-Paleo, F-59000 Lille, France
   Aix-Marseille Univ, CNRS, Centrale Marseille, iSm2, F-13013 Marseille, France
   Aix-Marseille Univ, CNRS, LISM, IMM FR3479, F-13009 Marseille, France
   Aix-Marseille Univ, CNRS, UMR7273, ICR, F-13013Marseille, France
   IFREMER Centre Brest REM/EEP/LEP, ZI de la Pointe du Diable, CS10070, F-29280Plouzané, France
   Sorbonne Université, CNRS, UMR 7144 AD2M, Station Biologique de Roscoff, Place Georges Teissier CS90074, F-29688 Roscoff, France
   Department of Applied and Molecular Microbiology, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany
C2 UNIV LILLE, FRANCE
   UNIV LILLE, FRANCE
   UNIV AIX MARSEILLE, FRANCE
   UNIV AIX MARSEILLE, FRANCE
   UNIV AIX MARSEILLE, FRANCE
   IFREMER, FRANCE
   UNIV PARIS 06, FRANCE
   UNIV BERLIN, GERMANY
SI BREST
SE PDG-REM-EEP-LEP
IN WOS Ifremer UPR
   DOAJ
   copubli-france
   copubli-europe
   copubli-univ-france
IF 1.103
TC 21
UR https://archimer.ifremer.fr/doc/00511/62307/66556.pdf
LA English
DT Article
CR CHUBACARC
   MESCAL
   MESCAL_LEG1
   MESCAL_LEG2
BO L'Atalante
DE ;Antibiotics;annelids;nematodes;AMP;extremophiles
AB Antimicrobial peptides (AMPs) are natural antibiotics produced by all living organisms. In metazoans, they act as host defense factors by eliminating microbial pathogens. But they also help to select the colonizing bacterial symbionts while coping with specific environmental challenges. Although many AMPs share common structural characteristics, for example having an overall size between 10–100 amino acids, a net positive charge, a γ-core motif, or a high content of cysteines, they greatly differ in coding sequences as a consequence of multiple parallel evolution in the face of pathogens. The majority of AMPs is specific of certain taxa or even typifying species. This is especially the case of annelids (ringed worms). Even in regions with extreme environmental conditions (polar, hydrothermal, abyssal, polluted, etc.), worms have colonized all habitats on Earth and dominated in biomass most of them while co-occurring with a large number and variety of bacteria. This review surveys the different structures and functions of AMPs that have been so far encountered in annelids and nematodes. It highlights the wide diversity of AMP primary structures and their originality that presumably mimics the highly diverse life styles and ecology of worms. From the unique system that represents marine annelids, we have studied the effect of abiotic pressures on the selection of AMPs and demonstrated the promising sources of antibiotics that they could constitute. 
PY 2019
PD SEP
SO Marine Drugs
SN 1660-3397
PU MDPI AG
VL 17
IS 9
UT 000487959700050
DI 10.3390/md17090512
ID 62307
ER

EF