FN Archimer Export Format
PT J
TI NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides
BT 
AF ROCH, Philippe
   YANG, Y
   TOUBIANA, Mylene
   AUMELAS, A
AS 1:1;2:2,3;3:1;4:2,3;
FF 1:;2:;3:;4:;
C1 Univ Montpellier 2, IFREMER, CNRS, UMR 5119, F-34095 Montpellier, France.
   Univ Montpellier 1, Ctr Biochim Struct, U554, INSERM,CNRS,UMR 5048, F-34090 Montpellier, France.
   Univ Montpellier 2, Ctr Biochim Struct, U554, INSERM,CNRS,UMR 5048, F-34090 Montpellier, France.
C2 CNRS, FRANCE
   UNIV MONTPELLIER, FRANCE
   UNIV MONTPELLIER, FRANCE
   IFREMER, FRANCE
SI MONTPELLIER
SE PDG-DRV-RA-DRIM
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 2.833
TC 54
UR https://archimer.ifremer.fr/doc/2008/publication-4485.pdf
LA English
DT Article
DE ;Shrimp;Molluscs;Mussel;Antibacterial activity;WSSV;Viral protection;Beta hairpin structure;NMR;Mytilin;Antimicrobial peptide
AB Mytilin is a 34-residue antibacterial peptide from the mussel Mytilus galloprovincialis, which in addition possesses in vitro antiviral activity. The three-dimensional solution structure of the synthetic mytilin was established by using 1H NMR and consists of the common cysteine-stabilized alpha beta motif close to the one observed in the mussel defensin MGD-1. Mytilin is characterized by 8 cysteines engaged in four disulfide bonds (2-27, 6-29, 10-31, and 15-34) only involving the beta-strand II. Hydrophilic and hydrophobic areas of mytilin account for 63% and 37%, respectively, a ratio very close to that of MGD-1 (64% and 36%). One linear and three cyclic fragments were designed from the interstrand loop sequence known to retain the biological activities in MGD-1. Only the fragment of 10 amino acids (C10C) constrained by two disulfide bonds in a stable beta-hairpin structure was able to inhibit the mortality of Palaemon serratus shrimp injected with white spot syndrome virus (WSSV). Fifty percent inhibition was obtained by in vitro pre-incubation of WSSV with 45 mu M of C10C compared with 7 mu M for mytilin. Interaction between the fragment and the virus occurred very rapidly as 40% survival was recorded after only 1 min of pre-incubation. In addition, C10C was capable of inhibiting in vitro growth of Vibrio splendidus LGP32 (MIC 125 mu M), Vibrio anguillarum (MIC 2mM), Micrococcus lysodeikticus and Escherichia coli (MIC 1 mM). Destroying the cysteine-stabilized alpha beta structure or shortening the C10C fragment to the C6C fragment with only one disulfide bond resulted in toss of both antiviral and antibacterial activities. Increasing the positive net charge did not enforce the antibacterial activity and completely suppressed the antiviral one. The C10C-designed peptide from mytilin appeared comparable in composition and structure with protegrin, tachyplesin and polyphemusin. (c) 2007 Elsevier Ltd. All rights reserved.
PY 2008
PD MAR
SO Developmental & Comparative Immunology
SN 0145-305X
PU Elsevier
VL 32
IS 3
UT 000252651500007
BP 227
EP 238
DI 10.1016/j.dci.2007.05.006
ID 4485
ER

EF