Structure of trichorzianine A IIIc, an antifungal peptide from Trichoderma harzianum

Bodo, Bernard; Rebuffat, Sylvie; Hajji, Mohamed El; Davoust, Daniel

doi:10.1021/ja00307a028

Cited by 92 publications

(41 citation statements)

References 6 publications

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“…Linear peptides containing a C-terminal amino alcohol, Lo1 (1 l), Phol (phenylalaninol) (12), or Trpol (tryptophanol) (13), and a high proportion of the unusual amino acid Aib (14) belong to the class of natural products known as peptaibols. The Trichodei-ma metabolites trichorzianine A (13), trichosporin B (12b,c,d), tricholongin BI and BII (1 la), trichogin A IV (1 lb), trichodecenins-I and -11 (1 1 4 , and the alamethicins (128 are among the best known peptaibols.…”

Section: Resultsmentioning

confidence: 99%

Peptaibol metabolites of Tolypocladium geodes

Tsantrizos¹,

Pischos²,

Sauriol³

et al. 1996

Can. J. Chem.

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Three antibiotic peptides, LP237-F8 (I), F5 (2), and F7 (3), were isolated from the liquid culture of the fungus Toly~>ocladi~imgeorlrs. Chemical shift assignments of the 'H and "C NMR resonances and sequencing of these metabolites were achieved by extensive high-field 2D NMR spectroscopy. The N-terminal of peptides 1 and 2 is protected with an octanoyl (Oc) fatty acid unit, whereas that of peptide 3 is protected with a decanoyl (Dec) unit. The C-terminal of all three peptides is protected with the amino alcohol leucinol (Lol). All three metabolites contain the common amino acids Ala, Phe or Tyr, Pro, and Gln, as well as the unusual amino acid a-aminoisobutyric acid (Aib). In addition, peptides 1 and 2 contain the amino acid a-amino-aethyl-12-pentanoic acid (a-ethylnorvaline, EtNor), which has not been previously reported as a constituent of a natural product. Metabolites 1 , 2 , and 3 are new members of the class of natural products known as peptaibols.Key rvords: Tolypoclrirlilirn geodes, peptaibols, leucinol, a-amino-a-ethyl-11-pentanoic acid.RCsumC : On a isole trois peptides antibiotiques, LP237-F8 (I), F5 (2) et F7 (3) h partir de milieux de culture liquides du champignon Tol.yl,oclndirirrl geodes. On a attribuC les deplacements chimiques des spectres RMN du 'H et du "C ainsi que la sequence de ces mitabolites en faisant un usage extensif de la spectroscopie RMN 2D ii haut champ. Le groupe N-terminal des peptides 1 et 2 est protege par une unite d'acide gras octanoyle (Oc) alors que celui du peptide 3 est protege par une unit6 dCcanoyle (Dec.) Le groupe C-terminal de chacun de ces trois peptides est protCgC par l'alcool amin6 leucinol (Lol). Les trois metabolites contiennent les acides arnines usuels Ala, PhC ou Tyr, Pro et Gin ainsi que I'acide a-aminoisobutyrique (Aib), un acide aniinC inhabituel. De plus, les peptides 1 et 2 contiennent l'acide aminC, a-amino-a-Cthyl-n-pentano'ique (a-Cthylnorvaline, EtNor), dont on n'a jamais rapport6 la presence comme constituant d'un produit naturel. Les mCtabolites 1 , 2 et 3 sont de nouveaux membres de la classe des produits naturels connus comme des peptaibols.Most clGs : Tolypocladi~irrl geodes, peptai'bols, leucinol, acide a-amino-a-ethyl-12-pentano'ique.[Traduit par la redaction]

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Section: Resultsmentioning

confidence: 99%

Peptaibol metabolites of Tolypocladium geodes

Tsantrizos¹,

Pischos²,

Sauriol³

et al. 1996

Can. J. Chem.

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“…The hinge around the Pro13 residue in tricholongins appears to be almost the same as in alamethicin. In spite of the very low temperature coefficient exhibited by the residue at position 3 (Phe3) which appears to be a common characteristic of peptaibol helices [3,5,231, the presence of a 310 bond at the beginning of the helix as previously suggested [3] is not clear from isotope-exchange rates. As the residue 3 follows a glycine in tricholongins and a proline in alamethicin, the presence of a Pro residue immediately before the residue 3 is not responsible for its low thermal coefficient and thus not required to cause a distortion in the N-terminal part of the helix.…”

Section: Secondary Structurementioning

confidence: 90%

Tricholongins BI and BII, 19‐residue peptaibols from Trichoderma longibrachiatum

Rebuffat

Prigent

Auvin‐Guette

et al. 1991

European Journal of Biochemistry

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Two nonadecapeptides, tricholongins BI and BII, which display antifungal and antibacterial activities, have been isolated from in vitro cultures of the fungus Trichoderma longibrachiatum. The peptides were separated by reversed-phase HPLC; their amino acid compositions were determined by gas chromatography and their sequences by positive-ion fast-atom-bombardment mass spectrometry and high-field NMR. These linear peptides, containing mainly hydrophobic L-amino acids, 8 -9 2-aminoisobutyric acid residues and exhibiting an acetylated N-terminal residue and an amino alcohol C-terminal leucinol belong to the peptaibol class. The methanol solution structure of tricholongins BI and BII has been investigated using both one-and two-dimensional NMR techniques. The total 'H-NMR and I3C-NMR assignments are given. By a combination of the 3 &~,~a~ coupling constant values, temperature coefficients of the NH and CO groups, amide hydrogen/deuterium-exchange rate measurements and NOE data, a secondary structure for tricholongins in solution has been proposed. Both peptides adopt a similar a-helical conformation with a hinge around Pro13 resulting from two 310 bonds. The results suggest that the Nterminus contains mixed a13 lobonds. The membrane permeability modifications induced by tricholongins have been assayed by the use of liposomes composed of egg phosphatidylcholine with 20-30% cholesterol. The peptide-induced leakage of an entrapped fluorescent probe has been followed by fluorescence spectroscopy. In a concentration range of 0.13-0.31 FM, tricholongins induce the leakage of 50% of the entrapped material in 20 min.The peptaibols include the well-known alamethicin from Trichoderma viride [I, 21 and trichorzianines from T. harzianum [3 -51. They are peptides of fungal origin whose mechanism of action is of interest, as they show a broad range of bioactivities. Structurally, these peptides contain an acetylated N-terminal residue, a C-terminal amino alcohol and a high percentage of hydrophobic amino acids including 2-aminoisobutyric acid (Aib).It is likely, therefore, that they are structurally related to melittin [6] or 6-haemolysin, extracted from bee venom and from Staphylococcus aureus, respectively, as they all exhibit a common tendency to form amphiphilic helices. It seems likely, also, that their mechanisms of action are close to those proposed to explain the interaction of melittin with biological membranes [7-101 and also the formation of voltage-gated ion channels [II, 121. We isolated two new groups of peptaibols form T. longibrachiatum (MNHN 3431), one composed of 19-residue neutral peptides and the other consisting of shorter sequences; these were named tricholongins and trichogins, respectively [I 31. These peptides exhibited both antifungal and antibacterial properties against various fungal strains and Grampositive bacteria. In this paper, we describe the isolation, sequence determination and conformational characteristics of the most abundant two peptides of the tricholongin group, tricholongins BI and BII...

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“…A single PCR product was obtained and used to probe a cosmid library of T. virens. 2 One cosmid, 40B7, had high sequence similarity to known peptide synthetases. A probe derived from cosmid 40B7 was used to identify a BAC clone, pDXG70, that was used for further analysis (25).…”

Section: Methodsmentioning

confidence: 99%

Identification of Peptaibols from Trichoderma virens and Cloning of a Peptaibol Synthetase

Wiest¹,

Grzegorski²,

Xu³

et al. 2002

Journal of Biological Chemistry

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214

173

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The fungus Trichoderma virens is a ubiquitous soil saprophyte that has been applied as a biological control agent to protect plants from fungal pathogens. One mechanism of biocontrol is mycoparasitism, and T. virens produces antifungal compounds to assist in killing its fungal targets. Peptide synthetases produce a wide variety of peptide secondary metabolites in bacteria and fungi. Many of these are known to possess antibiotic activities. Peptaibols form a class of antibiotics known for their high ␣-aminoisobutyric acid content and their synthesis as a mixture of isoforms ranging from 7 to 20 amino acids in length. Here we report preliminary characterization of a 62.8-kb continuous open reading frame encoding a peptaibol synthetase from T. virens. The predicted protein structure consists of 18 peptide synthetase modules with additional modifying domains at the N-and C-termini. T. virens was shown to produce a mixture of peptaibols, with the largest peptides being 18 residues. Mutation of the gene eliminated production of all peptaibol isoforms. Identification of the gene responsible for peptaibol production will facilitate studies of the structure and function of peptaibol antibiotics and their contribution to biocontrol activity.

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Structure of trichorzianine A IIIc, an antifungal peptide from Trichoderma harzianum

Cited by 92 publications

References 6 publications

Peptaibol metabolites of Tolypocladium geodes

Peptaibol metabolites of Tolypocladium geodes

Tricholongins BI and BII, 19‐residue peptaibols from Trichoderma longibrachiatum

Identification of Peptaibols from Trichoderma virens and Cloning of a Peptaibol Synthetase

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