Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger

被引:61
作者
Da Silva, P
Jouvensal, L
Lamberty, M
Bulet, P
Caille, A
Vovelle, F
机构
[1] Univ Orleans, CNRS, UPR 4301, Ctr Biophys Mol, F-45071 Orleans 2, France
[2] CNRS, Inst Biol Mol & Cellulaire, UPR 9022, F-67084 Strasbourg, France
关键词
termite; cysteine-rich; antimicrobial peptide; insect defensin; CS alpha beta motif; NMR;
D O I
10.1110/ps.0228303
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
The solution structure of termicin from hemocytes of the termite Pseudacanthotermes spiniger was determined by proton two-dimensional nuclear magnetic resonance spectroscopy and molecular modeling techniques. Termicin is a cysteine-rich antifungal peptide also exhibiting a weak antibacterial activity. The global fold of termicin consists of an alpha-helical segment (Phe4-Gln14) and a two-stranded (Phe19-Asp25 and Gln28-Phe33) antiparallel. beta-sheet forming a "cysteine stabilized alphabeta motif" (CSalphabeta) also found in antibacterial and antifungal defensins from insects and from plants. Interestingly, termicin shares more structural similarities with the antibacterial insect defensins and with MGD-1, a mussel defensin, than with the insect antifungal defensins such as drosomycin and heliomicin. These structural comparisons suggest that global fold alone does not explain the difference between antifungals and antibacterials. The antifungal properties of termicin may be related to its marked hydrophobicity and its amphipatic structure as compared to the antibacterial defensins. [SWISS-PROT accession number: Termicin (P82321); PDB accession number: 1MM0.].
引用
收藏
页码:438 / 446
页数:9
相关论文
共 50 条
[1]   Expression of insect cystein-rich antifungal peptides in transgenic tobacco enhances resistance to a fungal disease [J].
Banzet, N ;
Latorse, MP ;
Bulet, P ;
François, E ;
Derpierre, C ;
Dubald, M .
PLANT SCIENCE, 2002, 162 (06) :995-1006
[2]  
BARTELS C, 1995, J BIOMOL NMR, V5, P1
[3]   MLEV-17-BASED TWO-DIMENSIONAL HOMONUCLEAR MAGNETIZATION TRANSFER SPECTROSCOPY [J].
BAX, A ;
DAVIS, DG .
JOURNAL OF MAGNETIC RESONANCE, 1985, 65 (02) :355-360
[4]  
BEVINS CL, 2002, PEPTIDE ANTIBIOTICS
[5]   REFINED STRUCTURE OF CHARYBDOTOXIN - COMMON MOTIFS IN SCORPION TOXINS AND INSECT DEFENSINS [J].
BONTEMS, F ;
ROUMESTAND, C ;
GILQUIN, B ;
MENEZ, A ;
TOMA, F .
SCIENCE, 1991, 254 (5037) :1521-1523
[6]   SOLUTION STRUCTURE OF GAMMA-1-H AND GAMMA-1-P THIONINS FROM BARLEY AND WHEAT ENDOSPERM DETERMINED BY H-1-NMR - A STRUCTURAL MOTIF COMMON TO TOXIC ARTHROPOD PROTEINS [J].
BRUIX, M ;
JIMENEZ, MA ;
SANTORO, J ;
GONZALEZ, C ;
COLILLA, FJ ;
MENDEZ, E ;
RICO, M .
BIOCHEMISTRY, 1993, 32 (02) :715-724
[7]   Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].
Brunger, AT ;
Adams, PD ;
Clore, GM ;
DeLano, WL ;
Gros, P ;
Grosse-Kunstleve, RW ;
Jiang, JS ;
Kuszewski, J ;
Nilges, M ;
Pannu, NS ;
Read, RJ ;
Rice, LM ;
Simonson, T ;
Warren, GL .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 1998, 54 :905-921
[8]   Antimicrobial peptides in insects; structure and function [J].
Bulet, P ;
Hetru, C ;
Dimarcq, JL ;
Hoffmann, D .
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 1999, 23 (4-5) :329-344
[9]   A NOVEL INSECT DEFENSIN MEDIATES THE INDUCIBLE ANTIBACTERIAL ACTIVITY IN LARVAE OF THE DRAGONFLY AESCHNA-CYANEA (PALEOPTERA, ODONATA) [J].
BULET, P ;
COCIANCICH, S ;
REULAND, M ;
SAUBER, F ;
BISCHOFF, R ;
HEGY, G ;
VANDORSSELAER, A ;
HETRU, C ;
HOFFMANN, JA .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1992, 209 (03) :977-984
[10]   Solution structure of the thermostable sweet-tasting protein brazzein [J].
Caldwell, JE ;
Abildgaard, F ;
Dzakula, Z ;
Ming, D ;
Hellekant, G ;
Markley, JL .
NATURE STRUCTURAL BIOLOGY, 1998, 5 (06) :427-431