Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.

Fehlbaum, Pascale; Bulet, Philippe; Chernysh, Serguey; Briand, Jean‐Paul; Roussel, J.‐P.; Letellìer, Lucienne; Hétru, Charles; Hoffmann, Jules A.

doi:10.1073/pnas.93.3.1221

Cited by 278 publications

(281 citation statements)

References 20 publications

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“…It has not previously been reported that thanatin has antifungal activity against the rice blast pathogen M. oryzae, although this was expected because thanatin has wide-ranging activity against many kinds of fungi (Fehlbaum et al 1996). As shown in Fig.…”

Section: Acquired Resistance Of the Transformant To Rice Blastmentioning

confidence: 95%

“…Antimicrobial activity was determined as previously described, using Micrococcus luteus in 96-well microtiter plate, to which were added 10 g of crude plant extract or 10 l of the high-performance liquid chromatography ( Luteus (Fehlbaum et al 1996).…”

Section: Bioassay Of Antimicrobial Activitymentioning

confidence: 99%

“…Thanatin, produced in the stinkbug, the hemipteran insect Podisus maculiventris, is an AMP consisting of 21 amino acid residues (GSKKPVPIIYCNRRTGKCQRM) with a molecular weight of 2.4 kDa (Fehlbaum et al 1996). Thanatin is categorized as a -hairpin-type of AMP, which contains an internal disulfide bond.…”

Section: Introductionmentioning

confidence: 99%

“…In the last decade, acquired resistance to plant disease caused by a various pathogens, including fungi and bacteria, can be achieved by the introduction of AMPs into transgenic plants (Coca et al 2006;Mitsuhara et al 2000;Osusky et al 2004;Sharma et al 2000;Yevtushenko et al 2007). Thanatin has a wide-ranging antimicrobial spectrum, which includes many kinds of bacteria and fungi (Fehlbaum et al 1996). It is expected that thanatin can be used as a powerful antimicrobial substance in this system.…”

Section: Introductionmentioning

confidence: 99%

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Acquired resistance to the rice blast in transgenic rice accumulating the antimicrobial peptide thanatin

et al. 2009

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Thanatin is an antimicrobial peptide with a strong and wide-ranging antimicrobial spectrum, including certain species of fungi and Gram-negative and -positive bacteria. To evaluate the application of thanatin to the generation of disease-resistant plants, we introduced a synthetic thanatin gene into rice. Several transformants that expressed the introduced gene showed significant level of antimicrobial activity. The substances showing antimicrobial activity were partially purified from these transformants and their properties were determined. The molecule with characteristics similar to those of native thanatin on the elution pattern in HPLC analysis had an identical molecular mass to that of native molecule. It should also be noted that the transformant acquired a sufficient level of resistance to the rice blast fungus, Magnaporthe oryzae, presumably due to the repressive activity of thanatin to its initial stage of infection. This result demonstrates that thanatin has antifungal activity for M. oryzae and that the introduction of the thanatin gene into rice is effective in generating a plant resistant to rice blast disease.

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Section: Acquired Resistance Of the Transformant To Rice Blastmentioning

confidence: 95%

Section: Bioassay Of Antimicrobial Activitymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Acquired resistance to the rice blast in transgenic rice accumulating the antimicrobial peptide thanatin

et al. 2009

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“…(c) Thanatin Thanatin is a 21-residue cationic peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family (31,32). It has a single disulfide bridge and exhibits a remarkably large spectrum of activity against both Grampositive and Gram-negative bacteria and against filamentous fungi.…”

Section: (B) Drosomycinmentioning

confidence: 99%

Antimicrobial peptide defense in Drosophila

1997

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Drosophila responds to a septic injury by the rapid synthesis of antimicrobial peptides. These molecules are predominantly produced by the fat body, a functional equivalent of mammalian liver, and are secreted into the hemolymph where their concentrations can reach up to 100 μM. Six distinct antibacterial peptides (plus isoforms) and one antifungal peptide have been characterized in Drosophila and their genes cloned. The induction of the gene encoding the antifungal peptide relies on the spätzle/Toll/cactus gene cassette, which is involved in the control of dorsoventral patterning in the embryo, and shows interesting structural and functional similarities with cytokine‐induced activation of NF‐ϰB in mammalian cells. An additional pathway, dependent on the as yet unidentified imd (for immune‐deficiency) gene, is required for the full induction of the antibacterial peptide genes. Mutants deficient for the Toll and imd pathways exhibit a severely reduced survival to fungal and bacterial infections, respectively. Recent data on the molecular mechanisms underlying recognition of non‐self are also discussed in this review.

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The three-dimensional solution structure ofAesculus hippocastanum antimicrobial protein 1 determined by1H nuclear magnetic resonance

Fant¹,

Vranken²,

Borremans³

1999

Proteins

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Aesculus hippocastanum antimicrobial protein 1 (Ah-AMP1) is a plant defensin isolated from horse chestnuts. The plant defensins have been divided in several subfamilies according to their amino acid sequence homology. Ah-AMP1, belonging to subfamily A2, inhibits growth of a broad range of fungi. So far, a three-dimensional structure has been determined only for members of subfamilies A3 and B2. In order to understand activity and specificity of these plant defensins, the structure of a protein belonging to subfamily A2 is needed. We report the three-dimensional solution structure of Ah-AMP1 as determined from twodimensional 1 H nuclear magnetic resonance data. The structure features all the characteristics of the ''cysteine-stabilized ␣␤-motif.'' A comparison of the structure, the electrostatic potential surface and regions important for interaction with the fungal receptor, is made with Rs-AFP1 (plant defensin of subfamily A3). Thus, residues important for activity and specificity have been assigned. Proteins 1999;37:388-403.

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Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.

Cited by 278 publications

References 20 publications

Acquired resistance to the rice blast in transgenic rice accumulating the antimicrobial peptide thanatin

Acquired resistance to the rice blast in transgenic rice accumulating the antimicrobial peptide thanatin

Antimicrobial peptide defense in Drosophila

The three-dimensional solution structure ofAesculus hippocastanum antimicrobial protein 1 determined by1H nuclear magnetic resonance

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