Conformations in solution of the fuscopeptins

Bare, Simona; Coiro, V. M.; Scaloni, Andrea; Nola, Alfredo Di; Paci, Maurizio; Segre, Anna Laura; Ballio, A.

doi:10.1046/j.1432-1327.1999.00883.x

Cited by 12 publications

(3 citation statements)

References 28 publications

(41 reference statements)

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“…CD and NMR spectroscopy revealed that FPs are completely unstructured in aqueous solution with a large molecular flexibility, while in a membrane mimetic solution the peptidic region appears to adopt a helical structure [40]. These results are in line with those reported for Tol where a prevalence of helical structure was indeed observed in lipid membrane [15].…”

Section: Planar Lipid Membrane Experimentssupporting

confidence: 88%

Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes

Coraiola

Paletti

Fiore

et al. 2007

Journal of Peptide Science

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FP-A and FP-B are LDPs produced by the plant pathogen Pseudomonas fuscovaginae. As expected from their primary structure, they shared a similar mechanism of action with the better characterized SPs, synthesized by strains of Pseudomonas syringae pv. syringae. Indeed, they displayed hemolytic activity on human erythrocytes and were able to induce calcein release from LUVs: the effect was dependent on the concentration of the FPs and the lipid composition of the liposome and, in particular, it increased with the SM content of the membrane. The permeabilizing activity was further investigated on PLMs. FPs were able to open pores on pure POPC membranes. Pore opening was strongly voltage dependent: by switching the potential from negative to positive values, an increase in the absolute amplitude of transmembrane current was induced with simultaneous closure of pores. In 0.1 M KCl both FPs' pores had a conductance of 4 and 9 pS at −140 mV and +140 mV, respectively. Studies on ion selectivity indicated that FPs formed cation-selective channels.

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Section: Planar Lipid Membrane Experimentssupporting

confidence: 88%

Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes

Coraiola

Paletti

Fiore

et al. 2007

Journal of Peptide Science

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“…Phylogenetic analysis of condensation domains allows to distinguish lipoinitiation (C start ), regular ( L C L ) and coepimerization (C/E) domains. This enabled a comparison of the inferred peptide stereochemistry with the reported structure of fuscopeptin (fuscopeptin A/B: C8/10-OH Dhb - (Ballio et al, 1996;Baréet al, 1999) and syringotoxin (syringotoxin B: C14-OH L-Ser -D-Dab -Gly -D-Hse -L-Orn -L-aThr -Z-Dhb -L-Asp(OH) -Cl-L-Thr) (Flamand et al, 1996;Bender et al, 1999) (Figure 1 and S3). The bioinformatic prediction matched well with the experimental data, except for the configuration of two fuscopeptin residues, L-Leu3 and D-Dab18.…”

Section: P Fuscovaginae Upb0736 Harbors Three Bgcs For the Production...mentioning

confidence: 99%

Versatile role of Pseudomonas fuscovaginae cyclic lipopeptides in plant and microbial interactions

Ferrarini

Špacapan²,

Lam³

et al. 2022

Front. Plant Sci.

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Pseudomonas fuscovaginae is the most prominent bacterial sheath rot pathogen, causing sheath brown rot disease in rice. This disease occurs worldwide and it is characterized by typical necrotic lesions on the sheath, as well as a reduction in the number of emitted panicles and filled grains. P. fuscovaginae has been shown to produce syringotoxin and fuscopeptin cyclic lipopeptides (CLPs), which have been linked to pathogenicity. In this study, we investigated the role of P. fuscovaginae UPB0736 CLPs in plant pathogenicity, antifungal activity and swarming motility. To do so, we sequenced the strain to obtain a single-contig genome and we constructed deletion mutants in the biosynthetic gene clusters responsible for the synthesis of CLPs. We show that UPB0736 produces a third CLP of 13 amino acids, now named asplenin, and we link this CLP with the swarming activity of the strain. We could then show that syringotoxin is particularly active against Rhizoctonia solani in vitro. By testing the mutants in planta we investigated the role of both fuscopeptin and syringotoxin in causing sheath rot lesions. We proved that the presence of these two CLPs considerably affected the number of emitted panicles, although their number was still significantly affected in the mutants deficient in both fuscopeptin and syringotoxin. These results reveal the importance of CLPs in P. fuscovaginae pathogenicity, but also suggest that other pathogenicity factors may be involved.

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“…Both LPDs ( 14 and 15 ) showed phytotoxic and antifungal activity [ 31 ]. Their conformation in solution was also obtained by a NOE-NMR study [ 32 ].…”

Section: Source Isolation and Biological Activity Of Bacterial Lipode...mentioning

confidence: 99%

Bioactive Lipodepsipeptides Produced by Bacteria and Fungi

Evidente

2022

IJMS

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Natural products are a vital source for agriculture, medicine, cosmetics and other fields. Lipodepsipeptides (LPDs) are a wide group of natural products distributed among living organisms such as bacteria, fungi, yeasts, virus, insects, plants and marine organisms. They are a group of compounds consisting of a lipid connected to a peptide, which are able to self-assemble into several different structures. They have shown different biological activities such as phytotoxic, antibiotic, antiviral, antiparasitic, antifungal, antibacterial, immunosuppressive, herbicidal, cytotoxic and hemolytic activities. Their biological activities seem to be due to their interactions with the plasma membrane (MP) because they are able to mimic the architecture of the native membranes interacting with their hydrophobic segment. LPDs also have surfactant properties. The review has been focused on the lipodepsipeptides isolated from fungal and bacterial sources, on their biological activity, on the structure–activity relationships of some selected LPD subgroups and on their potential application in agriculture and medicine. The chemical and biological characterization of lipodepsipeptides isolated in the last three decades and findings that resulted from SCI-FINDER research are reported. A critical evaluation of the most recent reviews dealing with the same argument has also been described.

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Conformations in solution of the fuscopeptins

Cited by 12 publications

References 28 publications

Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes

Fuscopeptins, antimicrobial lipodepsipeptides from Pseudomonas fuscovaginae, are channel forming peptides active on biological and model membranes

Versatile role of Pseudomonas fuscovaginae cyclic lipopeptides in plant and microbial interactions

Bioactive Lipodepsipeptides Produced by Bacteria and Fungi

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