Antimicrobial Cyclic Peptides for Plant Disease Control

Lee, Dong Wan; Kim, Beom Seok

doi:10.5423/ppj.rw.08.2014.0074

Cited by 46 publications

(35 citation statements)

References 90 publications

(90 reference statements)

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“…The 1 H, 13 C, and DEPT 135 NMR spectra of 3 were similar to those of 2, and the main differences between them were the additional presence of a keto carbonyl group at δ C 208.5, the downfield shifts of a methylene [δ H 2.38 (2H, t, J = 7.5 Hz), δ C 42.6] and a methyl [δ H 2.05 (3H, s), δ C 29.6], and the absence of two methylene signals and a methyl group in 3. In the HMBC spectrum, the key correlations of H-12 (δ H 2.38, t, J = 7.5 Hz) and H-14 (δ H 2.05, s) with C-13 (δ C 208.5, C), and H-14 with C-12 (δ C 29.6, CH 2 ), combined with other HMBC correlations and Figure 3) suggested that 3 also contained six amino acid residues including a Val instead of an Ile, a Tyr, a Gln, a Pro, an Ala, and a Thr, and the sequence of the amino acid residues was ValTyr-Gln-Pro-Ala-Thr-HKTA.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Verlamelin A is a cyclic hexadepsipeptide antibiotic originally isolated from Verticillium lamellicola in 1980 11 with antifungal activity toward phytopathogenic fungi in vitro and in vivo; 13,14 then it was also isolated from an entomopathogenic fungus Lecanicillium sp. HF627 in 2014 together with its analogue verlamelin B, and its absolute configuration was determined for the first time.…”

Section: ■ Introductionmentioning

confidence: 99%

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Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020

Xiao

Nong

Huang

et al. 2017

J. Agric. Food Chem.

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A new linear peptide simplicilliumtide I (1) and four new cyclic peptides simplicilliumtides J−M (2−5) together with known analogues verlamelins A and B (6 and 7) were isolated from the deep-sea-derived fungal strain Simplicillium obclavatum EIODSF 020. Their structures were elucidated by spectroscopic analysis, and their absolute configurations were further confirmed by chemical structural modification, Marfey's and Mosher's methods. Compounds 2, 6, and 7 showed significant antifungal activity toward Aspergillus versicolor and Curvularia australiensis and also had obvious antiviral activity toward HSV-1 with IC 50 values of 14.0, 16.7, and 15.6 μM, respectively. The structure−bioactivity relationship of this type of cyclic peptide was also discussed. This is the first time to discuss the effects of the lactone linkage and the substituent group of the fatty acid chain fragment on the bioactivity of this type of cyclic peptides. This is also the first time to report the antiviral activity of these cyclic peptides. KEYWORDS: deep-sea-derived fungus, Simplicillium obclavatum, peptide, antifungal, antiviral, structure−bioactivity relationshipFungi are important sources of novel bioactive compounds that are considered to be interesting synthetic models or important new lead compounds for medicine as well as for plant protection.1−5 Fungus Simplicillium lamellicola, previously known as Acremonium strictum BCP, was lately given the name based on 28S rRNA gene and ITS regions. A. strictum BCP could produce cyclic hexapeptide verlamelin 6 and was used as a microbial fungicide with the mechanism of mycoparasitism and antibiosis. 7−9 In our previous study, we had found eight linear peptides (namely, simplicilliumtides A− H) from a deep-sea-derived fungal strain Simplicillium obclavatum EIODSF 020. 10 Now, in our continued study, a new linear peptide simplicilliumtide I (1) and four new cyclic hexapeptides simplicilliumtides J−M (2−5) together with known analogues verlamelins A and B (6 and 7)11,12 were further isolated from the same crude extract of the fungal strain (Figure 1). Verlamelin A is a cyclic hexadepsipeptide antibiotic originally isolated from Verticillium lamellicola in 1980 11 with antifungal activity toward phytopathogenic fungi in vitro and in vivo;13,14 then it was also isolated from an entomopathogenic fungus Lecanicillium sp. HF627 in 2014 together with its analogue verlamelin B, and its absolute configuration was determined for the first time.12 At the same time a gene cluster responsible for the biosynthesis of verlamelin was also identified. 15 In this article, we report the isolation, structure elucidation, and antifungal and antiviral activities of the peptides (1−7). Their structure−bioactivity relationship is also discussed. ■ MATERIALS AND METHODSGeneral Experimental Procedures. The procedures were the same as previously reported.10 Details are described in the Supporting Information.

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Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020

Xiao

Nong

Huang

et al. 2017

J. Agric. Food Chem.

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“…The involvement of lipopeptides in the control of plant pathogens by B. amyloliquefaciens and B. subtilis has been well recognized . Recently, Romero et al .…”

Section: Discussionmentioning

confidence: 99%

Importance of prumycin produced by Bacillus amyloliquefaciens SD‐32 in biocontrol against cucumber powdery mildew disease

Tanaka

Fukuda

Amaki

et al. 2017

Pest Management Science

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“…The cationic nature of AMPs determines their ability to interact selectively with negatively charged microbial surfaces, which result in disruption or inhibition of microbial cells [3] [4] [5].…”

Section: Introductionmentioning

confidence: 99%

Expression of Fusion Lytic Peptides Promotes Fungal Disease Resistance in Transgenic Plants

Biliarski¹,

Yertaeva²,

Mitra³

2020

AJPS

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Many organisms produce small proteins which exhibit antimicrobial activities. In recent decades, the biological role of antimicrobial peptides (AMP) has been recognized as the main factor in the defense mechanisms against a broad range of pathogenic microbes. The increased worldwide incidence of microbial resistance to antibiotics makes AMPs promising alternative for the control of microbial disease. Exploring the potential of AMPs in transgenic crops could lead to the development of new and improved cultivars which are resistant to various economically important diseases. In the present study, two fusion lytic peptide gene constructs coding for antimicrobial peptides were expressed in Nicotiana benthamiana tobacco plants and tested against three fungal pathogens, Sclerotinia sclerotiorum, Rhizoctonia solani, and Pythium sp. Detached-leaf bioassay was employed for the transgenic plants carrying the fusion lytic peptide constructs (ORF13 and RSA1), transgenic vector only control plants (1234), and wild-type control plants (WT) against the three fungal pathogens. Symptom area of each leaf was measured with high accuracy and data were recorded and processed by statistical analyses. The results showed that transgenic plant lines ORF13 and RSL1 have substantial resistance to Sclerotinia sclerotiorum infection, producing significantly smaller lesion areas compared to vector only plant line 1234 and wild type plants.These transgenic lines also provided resistance against Rhizoctonia solani, however, these lines were not effective against the other fungal pathogen Pythium sp.

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Antimicrobial Cyclic Peptides for Plant Disease Control

Cited by 46 publications

References 90 publications

Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020

Antifungal and Antiviral Cyclic Peptides from the Deep-Sea-Derived Fungus Simplicillium obclavatum EIODSF 020

Importance of prumycin produced by Bacillus amyloliquefaciens SD‐32 in biocontrol against cucumber powdery mildew disease

Expression of Fusion Lytic Peptides Promotes Fungal Disease Resistance in Transgenic Plants

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