PURIFICATION AND CHARACTERIZATION OF A SCORPION DEFENSIN, A 4KDA ANTIBACTERIAL PEPTIDE PRESENTING STRUCTURAL SIMILARITIES WITH INSECT DEFENSINS AND SCORPION TOXINS

被引:145
作者
COCIANCICH, S
GOYFFON, M
BONTEMS, F
BULET, P
BOUET, F
MENEZ, A
HOFFMANN, J
机构
[1] MUSEUM NATL HIST NAT,ETUD & RECH ARTHROPODES IRRADIES LAB,F-75231 PARIS 05,FRANCE
[2] CRSSA,DIV BIOL GEN & ECOL,F-75005 PARIS,FRANCE
[3] CEA,CTR SACLAY,DEPT INGN & ETUD PROT,F-91191 GIF SUR YVETTE,FRANCE
关键词
D O I
10.1006/bbrc.1993.1778
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Insect defensins are a group of inducible small-sized antibacterial peptides with three intramolecular disulfide bridges. NMR studies have recently shown that they share striking structural similarities with scorpion toxins. We have investigated in a scorpion species, Leiurus quinquestriatus, the potential presence of antibacterial molecules and report the isolation and structural characterization of a novel insect defensin homologue, which we refer to as scorpion defensin. This peptide shows a remarkably high degree of sequence homology with a defensin recently characterized in a species belonging to the ancient insect order of the Odonata with which it defines a novel ancient subclass of defensins. The scorpion defensin has in common with the scorpion toxins a consensus sequence Cys-[.]-Cys-Xaa-Xaa-Xaa-Cys-[.]-Gly-Xaa-Cys-[.]-Cys-Xaa-Cys present in all scorpion toxins characterized so far. © 1993 Academic Press.
引用
收藏
页码:17 / 22
页数:6
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