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Titolo:
Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities
Autore:
Lamberty, M; Caille, A; Landon, C; Tassin-Moindrot, S; Hetru, C; Bulet, P; Vovelle, F;
Indirizzi:
Univ Orleans, CNRS, UPR 4301, Ctr Biophys Mol, F-45071 Orleans 2, France Univ Orleans Orleans France 2 Ctr Biophys Mol, F-45071 Orleans 2, France CNRS, Inst Biol Mol & Cellulaire, UPR 9022, F-67084 Strasbourg, France CNRS Strasbourg France F-67084 ire, UPR 9022, F-67084 Strasbourg, France
Titolo Testata:
BIOCHEMISTRY
fascicolo: 40, volume: 40, anno: 2001,
pagine: 11995 - 12003
SICI:
0006-2960(20011009)40:40<11995:SSOTAH>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
3-DIMENSIONAL SOLUTION STRUCTURE; NUCLEAR-MAGNETIC-RESONANCE; ANTIMICROBIAL PEPTIDES; PROTEIN STRUCTURES; SCORPION TOXINS; INSECT DEFENSIN; NMR; IMMUNITY; H-1-NMR; PROGRAM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Vovelle, F Univ Orleans, CNRS, UPR 4301, Ctr Biophys Mol, Rue Charles Sadron, F-45071Orleans 2, France Univ Orleans Rue Charles Sadron Orleans France 2 ans 2, France
Citazione:
M. Lamberty et al., "Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities", BIOCHEM, 40(40), 2001, pp. 11995-12003

Abstract

In response to an experimental infection, the lepidopteran Heliothis virescens produces an antifungal protein named heliomicin. Heliomicin displays sequence similarities with antifungal plant defensins and antibacterial or antifungal insect defensins. To gain information about the structural elements required for either antifungal or antibacterial activity, heliomicin andselected point-mutated variants were expressed in yeast as fusion proteins. The effects of mutations, defined by comparing the primary structure of heliomicin with the sequences of members of the insect defensin family, wereanalyzed using antibacterial and antifungal assays. One of the variants shows significant activity against Gram-positive bacteria while remaining efficient against fungi. The three-dimensional structures of this variant and of the wild-type protein were determined by two-dimensional H-1 NMR to establish a correlation between structure and antibacterial or antifungal activity. Wild-type and mutated heliomicins adopt a similar scaffold, including the so-called cysteine-stabilized alpha beta motif. A comparison of their structures with other defensin-type molecules indicates that common hydrophobic characteristics can be assigned to all the antifungal proteins. A comparative analysis of various structural features of heliomicin mutant and of antibacterial defensins enables common properties to be assessed, which will help to design new mutants with increased antibacterial activity.

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Documento generato il 01/12/20 alle ore 00:58:51