FN Archimer Export Format
PT J
TI NMR Structure of rALF-Pm3, an Anti-Lipopolysaccharide Factor from Shrimp: Model of the Possible Lipid A-Binding Site
BT 
AF YANG, Yinshan
   BOZE, Helene
   CHEMARDIN, Patrick
   PADILLA, Andre
   MOULIN, Guy
   TASSANAKAJON, Anchalee
   PUGNIERE, Martine
   ROQUET, Francoise
   DESTOUMIEUX GARZON, Delphine
   GUEGUEN, Yannick
   BACHERE, Evelyne
   AUMELAS, Andre
AS 1:1;2:2;3:2;4:1;5:2;6:3;7:4;8:4;9:5;10:5;11:5;12:1;
FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:PDG-DOP-DCOP-AQUAPOL-LBQP;11:PDG-DOP-DCM-BOME;12:;
C1 Univ Montpellier 1 & 2, INSERM, CNRS,U554, Ctr Biochim Struct,UMR5048, F-34090 Montpellier 9, France.
   Genie Microbiol & Enzymat, UMR SPO INRA, F-34060 Montpellier, France.
   Chulalongkorn Univ, Fac Sci, Dept Biochem, Shrimp Mol Biol & Genom Lab, Bangkok 10330, Thailand.
   Univ Montpellier 1, CPBS, F-34095 Montpellier, France.
   Univ Montpellier 2, CNRS, UMR Ecosyst Lagunaires 5119, IFREMER, F-34095 Montpellier 5, France.
C2 CNRS, FRANCE
   INRA, FRANCE
   UNIV CHULALONGKORN, THAILAND
   UNIV MONTPELLIER, FRANCE
   IFREMER, FRANCE
SI MONTPELLIER
   TAHITI
   PALAVAS
SE PDG-DOP-DCM-BOME-LALR
   PDG-DOP-DCOP-AQUAPOL-LBQP
   PDG-DOP-DCM-BOME
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-p187
   copubli-univ-france
   copubli-int-hors-europe
   copubli-sud
IF 2.605
TC 63
UR https://archimer.ifremer.fr/doc/2009/publication-6320.pdf
LA English
DT Article
DE ;Ultracentrifugation;Surface plasmon resonance;Septic shock;Structure;NMR;Lipid A;Lipopolysaccharide;Anti lipopolysaccharide factor
AB The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which prevented us to experimentally determine by NMR the binding mode of these lipids to rALF-Pm3. However, on the basis of striking structural similarities to the FhuA/LPS complex, we designed an original model of the possible lipid A-binding site of ALF-Pm3. Such a binding site, located on the ALF-Pm3 beta-sheet and involving seven charged residues, is well conserved in ALF-L from Limulus polyphemus and in ALF-T from Tachypleus tridentatus. In addition, our model is in agreement with experiments showing that beta-hairpin synthetic peptides corresponding to ALF-L beta-sheet bind to LPS. Delineating lipid A-binding site of ALFs will help go further in the de novo design of new antibacterial or LPS-neutralizing drugs. (C) 2008 Wiley Periodicals, Inc. Biopolymers 91: 207-220, 2009.
PY 2009
PD MAR
SO Biopolymers
SN 0006-3525
PU Wiley / Blackwell
VL 91
IS 3
UT 000262540400004
BP 207
EP 220
DI 10.1002/bip.21119
ID 6320
ER

EF