Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A

Andrea Scaloni, Mauro Dalla Serra, Pietro Amodeo, Luisa Mannina, Rosa Maria Vitale, Anna Laura Segre, Oscar Cruciani, Francesca Lodovichetti, Maria Luigia Greco, Alberto Fiore, Monica Gallo, Chiara D'Ambrosio, Manuela Coraiola, Gianfranco Menestrina, Antonio Graniti, Vincenzo Fogliano*

*Corresponding author for this work

Research output: Contribution to journalArticle

57 Citations (Scopus)

Abstract

Cationic lipodepsipeptides from Pseudomonas spp. have been characterized for their structural and antimicrobial properties. In the present study, the structure of a novel lipodepsipeptide, cormycin A, produced in culture by the tomato pathogen Pseudomonas corrugata was elucidated by combined protein chemistry, mass spectrometry and two-dimensional NMR procedures. Its peptide moiety corresponds to L-Ser-D-Orn-L-Asn-D-Hse-L-His-L-aThr-Z-Dhb-L-Asp(3-OH)-L- Thr(4-Cl) [where Orn represents ornithine, Hse ishomoserine, aThr is allo-threonine, Z-Dhb is 2,3-dehydro-2-aminobutanoic acid, Asp(3-OH) is 3-hydroxyaspartic acid and Thr(4-Cl) is 4-chlorothreonine], with the terminal carboxy group closing a macrocyclic ring with the hydroxy group of the N-terminal serine residue. This is, in turn, N-acylated by 3,4-dihydroxy- esadecanoate. In aqueous solution, cormycin A showed a rather compact structure, being derived from an inward orientation of some amino acid side chains and from the 'hairpin-bent' conformation of the lipid, due to inter-residue interactions involving its terminal part. Cormycin was significantly more active than the other lipodepsipeptides from Pseudomonas spp., as demonstrated by phytotoxicity and antibiosis assays, as well as by red-blood-cell lysis. Differences in biological activity were putatively ascribed to its weak positive net charge at neutral pH. Planar lipid membrane experiments showed step-like current transitions, suggesting that cormycin is able to form pores. This ability was strongly influenced by the phospholipid composition of the membrane and, in particular, by the presence of sterols. All of these findings suggest that cormycin derivatives could find promising applications, either as antifungal compounds for topical use or as post-harvest biocontrol agents.

Original languageEnglish
Pages (from-to)25-36
Number of pages12
JournalBiochemical Journal
Volume384
Issue number1
DOIs
Publication statusPublished - 15 Nov 2004
Externally publishedYes

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Pseudomonas
Bioactivity
Conformations
Biocontrol
Ornithine
Pathogens
Sterols
Threonine
Membrane Lipids
Antibiosis
Serine
Mass spectrometry
Assays
Phospholipids
Blood
Nuclear magnetic resonance
Lycopersicon esculentum
Viperidae
Derivatives
Membranes

Cite this

Scaloni, A., Dalla Serra, M., Amodeo, P., Mannina, L., Vitale, R. M., Segre, A. L., ... Fogliano, V. (2004). Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A. Biochemical Journal, 384(1), 25-36. https://doi.org/10.1042/BJ20040422
Scaloni, Andrea ; Dalla Serra, Mauro ; Amodeo, Pietro ; Mannina, Luisa ; Vitale, Rosa Maria ; Segre, Anna Laura ; Cruciani, Oscar ; Lodovichetti, Francesca ; Greco, Maria Luigia ; Fiore, Alberto ; Gallo, Monica ; D'Ambrosio, Chiara ; Coraiola, Manuela ; Menestrina, Gianfranco ; Graniti, Antonio ; Fogliano, Vincenzo. / Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata : cormycin A. In: Biochemical Journal. 2004 ; Vol. 384, No. 1. pp. 25-36.
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abstract = "Cationic lipodepsipeptides from Pseudomonas spp. have been characterized for their structural and antimicrobial properties. In the present study, the structure of a novel lipodepsipeptide, cormycin A, produced in culture by the tomato pathogen Pseudomonas corrugata was elucidated by combined protein chemistry, mass spectrometry and two-dimensional NMR procedures. Its peptide moiety corresponds to L-Ser-D-Orn-L-Asn-D-Hse-L-His-L-aThr-Z-Dhb-L-Asp(3-OH)-L- Thr(4-Cl) [where Orn represents ornithine, Hse ishomoserine, aThr is allo-threonine, Z-Dhb is 2,3-dehydro-2-aminobutanoic acid, Asp(3-OH) is 3-hydroxyaspartic acid and Thr(4-Cl) is 4-chlorothreonine], with the terminal carboxy group closing a macrocyclic ring with the hydroxy group of the N-terminal serine residue. This is, in turn, N-acylated by 3,4-dihydroxy- esadecanoate. In aqueous solution, cormycin A showed a rather compact structure, being derived from an inward orientation of some amino acid side chains and from the 'hairpin-bent' conformation of the lipid, due to inter-residue interactions involving its terminal part. Cormycin was significantly more active than the other lipodepsipeptides from Pseudomonas spp., as demonstrated by phytotoxicity and antibiosis assays, as well as by red-blood-cell lysis. Differences in biological activity were putatively ascribed to its weak positive net charge at neutral pH. Planar lipid membrane experiments showed step-like current transitions, suggesting that cormycin is able to form pores. This ability was strongly influenced by the phospholipid composition of the membrane and, in particular, by the presence of sterols. All of these findings suggest that cormycin derivatives could find promising applications, either as antifungal compounds for topical use or as post-harvest biocontrol agents.",
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Scaloni, A, Dalla Serra, M, Amodeo, P, Mannina, L, Vitale, RM, Segre, AL, Cruciani, O, Lodovichetti, F, Greco, ML, Fiore, A, Gallo, M, D'Ambrosio, C, Coraiola, M, Menestrina, G, Graniti, A & Fogliano, V 2004, 'Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A', Biochemical Journal, vol. 384, no. 1, pp. 25-36. https://doi.org/10.1042/BJ20040422

Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata : cormycin A. / Scaloni, Andrea; Dalla Serra, Mauro; Amodeo, Pietro; Mannina, Luisa; Vitale, Rosa Maria; Segre, Anna Laura; Cruciani, Oscar; Lodovichetti, Francesca; Greco, Maria Luigia; Fiore, Alberto; Gallo, Monica; D'Ambrosio, Chiara; Coraiola, Manuela; Menestrina, Gianfranco; Graniti, Antonio; Fogliano, Vincenzo.

In: Biochemical Journal, Vol. 384, No. 1, 15.11.2004, p. 25-36.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata

T2 - cormycin A

AU - Scaloni, Andrea

AU - Dalla Serra, Mauro

AU - Amodeo, Pietro

AU - Mannina, Luisa

AU - Vitale, Rosa Maria

AU - Segre, Anna Laura

AU - Cruciani, Oscar

AU - Lodovichetti, Francesca

AU - Greco, Maria Luigia

AU - Fiore, Alberto

AU - Gallo, Monica

AU - D'Ambrosio, Chiara

AU - Coraiola, Manuela

AU - Menestrina, Gianfranco

AU - Graniti, Antonio

AU - Fogliano, Vincenzo

PY - 2004/11/15

Y1 - 2004/11/15

N2 - Cationic lipodepsipeptides from Pseudomonas spp. have been characterized for their structural and antimicrobial properties. In the present study, the structure of a novel lipodepsipeptide, cormycin A, produced in culture by the tomato pathogen Pseudomonas corrugata was elucidated by combined protein chemistry, mass spectrometry and two-dimensional NMR procedures. Its peptide moiety corresponds to L-Ser-D-Orn-L-Asn-D-Hse-L-His-L-aThr-Z-Dhb-L-Asp(3-OH)-L- Thr(4-Cl) [where Orn represents ornithine, Hse ishomoserine, aThr is allo-threonine, Z-Dhb is 2,3-dehydro-2-aminobutanoic acid, Asp(3-OH) is 3-hydroxyaspartic acid and Thr(4-Cl) is 4-chlorothreonine], with the terminal carboxy group closing a macrocyclic ring with the hydroxy group of the N-terminal serine residue. This is, in turn, N-acylated by 3,4-dihydroxy- esadecanoate. In aqueous solution, cormycin A showed a rather compact structure, being derived from an inward orientation of some amino acid side chains and from the 'hairpin-bent' conformation of the lipid, due to inter-residue interactions involving its terminal part. Cormycin was significantly more active than the other lipodepsipeptides from Pseudomonas spp., as demonstrated by phytotoxicity and antibiosis assays, as well as by red-blood-cell lysis. Differences in biological activity were putatively ascribed to its weak positive net charge at neutral pH. Planar lipid membrane experiments showed step-like current transitions, suggesting that cormycin is able to form pores. This ability was strongly influenced by the phospholipid composition of the membrane and, in particular, by the presence of sterols. All of these findings suggest that cormycin derivatives could find promising applications, either as antifungal compounds for topical use or as post-harvest biocontrol agents.

AB - Cationic lipodepsipeptides from Pseudomonas spp. have been characterized for their structural and antimicrobial properties. In the present study, the structure of a novel lipodepsipeptide, cormycin A, produced in culture by the tomato pathogen Pseudomonas corrugata was elucidated by combined protein chemistry, mass spectrometry and two-dimensional NMR procedures. Its peptide moiety corresponds to L-Ser-D-Orn-L-Asn-D-Hse-L-His-L-aThr-Z-Dhb-L-Asp(3-OH)-L- Thr(4-Cl) [where Orn represents ornithine, Hse ishomoserine, aThr is allo-threonine, Z-Dhb is 2,3-dehydro-2-aminobutanoic acid, Asp(3-OH) is 3-hydroxyaspartic acid and Thr(4-Cl) is 4-chlorothreonine], with the terminal carboxy group closing a macrocyclic ring with the hydroxy group of the N-terminal serine residue. This is, in turn, N-acylated by 3,4-dihydroxy- esadecanoate. In aqueous solution, cormycin A showed a rather compact structure, being derived from an inward orientation of some amino acid side chains and from the 'hairpin-bent' conformation of the lipid, due to inter-residue interactions involving its terminal part. Cormycin was significantly more active than the other lipodepsipeptides from Pseudomonas spp., as demonstrated by phytotoxicity and antibiosis assays, as well as by red-blood-cell lysis. Differences in biological activity were putatively ascribed to its weak positive net charge at neutral pH. Planar lipid membrane experiments showed step-like current transitions, suggesting that cormycin is able to form pores. This ability was strongly influenced by the phospholipid composition of the membrane and, in particular, by the presence of sterols. All of these findings suggest that cormycin derivatives could find promising applications, either as antifungal compounds for topical use or as post-harvest biocontrol agents.

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DO - 10.1042/BJ20040422

M3 - Article

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VL - 384

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JO - Biochemical Journal

JF - Biochemical Journal

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