Antimicrobial lipodepsipeptides from Pseudomonas spp: a comparison of their activity on model membranes

G Menestrina*, M Coraiola, V. Fogliano, A Fiore, I. Grgurina, A Carpaneto, F Gambale, MD Serra

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.

Original languageEnglish
Title of host publicationPseudomonas syringae and related pathogens
Subtitle of host publicationbiology and genetic
EditorsNicola Sante Iacobellis, Alan Collmer, Steven W. Hutcheson, John W. Mansfield, Cindy E. Morris, Jesus Murillo, Norman W. Schaad, David E. Stead, Giuseppe Surico, Matthias S. Ullrich
Place of PublicationDordrecht
PublisherSpringer
Pages185-198
Number of pages14
ISBN (Electronic)9789401701334
ISBN (Print)9781402012273, 9789048162673
DOIs
Publication statusPublished - 2003
Externally publishedYes
Event6th International Conference on Pseudomonas Syringae Pathovars and Related Pathogens - Maratea, Italy
Duration: 15 Sep 200219 Sep 2002
Conference number: 6

Conference

Conference6th International Conference on Pseudomonas Syringae Pathovars and Related Pathogens
CountryItaly
CityMaratea
Period15/09/0219/09/02

Cite this

Menestrina, G., Coraiola, M., Fogliano, V., Fiore, A., Grgurina, I., Carpaneto, A., ... Serra, MD. (2003). Antimicrobial lipodepsipeptides from Pseudomonas spp: a comparison of their activity on model membranes. In N. S. Iacobellis, A. Collmer, S. W. Hutcheson, J. W. Mansfield, C. E. Morris, J. Murillo, N. W. Schaad, D. E. Stead, G. Surico, ... M. S. Ullrich (Eds.), Pseudomonas syringae and related pathogens: biology and genetic (pp. 185-198). Dordrecht: Springer. https://doi.org/10.1007/978-94-017-0133-4_20
Menestrina, G ; Coraiola, M ; Fogliano, V. ; Fiore, A ; Grgurina, I. ; Carpaneto, A ; Gambale, F ; Serra, MD. / Antimicrobial lipodepsipeptides from Pseudomonas spp : a comparison of their activity on model membranes. Pseudomonas syringae and related pathogens: biology and genetic. editor / Nicola Sante Iacobellis ; Alan Collmer ; Steven W. Hutcheson ; John W. Mansfield ; Cindy E. Morris ; Jesus Murillo ; Norman W. Schaad ; David E. Stead ; Giuseppe Surico ; Matthias S. Ullrich. Dordrecht : Springer, 2003. pp. 185-198
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title = "Antimicrobial lipodepsipeptides from Pseudomonas spp: a comparison of their activity on model membranes",
abstract = "Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.",
author = "G Menestrina and M Coraiola and V. Fogliano and A Fiore and I. Grgurina and A Carpaneto and F Gambale and MD Serra",
year = "2003",
doi = "10.1007/978-94-017-0133-4_20",
language = "English",
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pages = "185--198",
editor = "Iacobellis, {Nicola Sante} and Alan Collmer and Hutcheson, {Steven W.} and Mansfield, {John W.} and Morris, {Cindy E.} and Jesus Murillo and Schaad, {Norman W.} and Stead, {David E.} and Giuseppe Surico and Ullrich, {Matthias S.}",
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}

Menestrina, G, Coraiola, M, Fogliano, V, Fiore, A, Grgurina, I, Carpaneto, A, Gambale, F & Serra, MD 2003, Antimicrobial lipodepsipeptides from Pseudomonas spp: a comparison of their activity on model membranes. in NS Iacobellis, A Collmer, SW Hutcheson, JW Mansfield, CE Morris, J Murillo, NW Schaad, DE Stead, G Surico & MS Ullrich (eds), Pseudomonas syringae and related pathogens: biology and genetic. Springer, Dordrecht, pp. 185-198, 6th International Conference on Pseudomonas Syringae Pathovars and Related Pathogens, Maratea, Italy, 15/09/02. https://doi.org/10.1007/978-94-017-0133-4_20

Antimicrobial lipodepsipeptides from Pseudomonas spp : a comparison of their activity on model membranes. / Menestrina, G; Coraiola, M; Fogliano, V.; Fiore, A; Grgurina, I.; Carpaneto, A; Gambale, F; Serra, MD.

Pseudomonas syringae and related pathogens: biology and genetic. ed. / Nicola Sante Iacobellis; Alan Collmer; Steven W. Hutcheson; John W. Mansfield; Cindy E. Morris; Jesus Murillo; Norman W. Schaad; David E. Stead; Giuseppe Surico; Matthias S. Ullrich. Dordrecht : Springer, 2003. p. 185-198.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

TY - GEN

T1 - Antimicrobial lipodepsipeptides from Pseudomonas spp

T2 - a comparison of their activity on model membranes

AU - Menestrina, G

AU - Coraiola, M

AU - Fogliano, V.

AU - Fiore, A

AU - Grgurina, I.

AU - Carpaneto, A

AU - Gambale, F

AU - Serra, MD

PY - 2003

Y1 - 2003

N2 - Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.

AB - Lipodepsipeptides (LPDs) are a group of cyclic, acylated peptides produced by several Pseudomonas species. They are usually divided in two groups, mycins and peptins, on the basis of the size of the amino acidic part of the molecule. Mycins have a ring of 9 amino acids closed between the first and the last residue, peptins contain a more complex peptide moiety of up to 25 amino acids, partially cyclized. Both mycins and peptins attack the plasma membrane, but may have different target organisms. Comparing the mode of action of these two classes of LDPs on natural and model membranes we observed that all peptides induced red blood cell haemolysis and leakage of tonoplasts and liposornes by the formation of pores. The haemolytic activity of the smaller mycins was higher than that of the bigger peptins and proportional to the amphipathic index of the molecule. The extent of permeabilization was dependent also on the composition of the lipid membrane. In particular, mycins show a preference for sterols, whereas peptins are more active on phospholipids, especially sphingomyelin. These differences may have physiological implications. The formation of discrete ion channels, with anionic selectivity, was directly demonstrated by electrophysiological experiments performed on planar lipid bilayers or sugar beet vacuoles. The channels show sub-states and their properties in vacuoles and in planar lipid membranes were remarkably similar.

U2 - 10.1007/978-94-017-0133-4_20

DO - 10.1007/978-94-017-0133-4_20

M3 - Conference contribution

SN - 9781402012273

SN - 9789048162673

SP - 185

EP - 198

BT - Pseudomonas syringae and related pathogens

A2 - Iacobellis, Nicola Sante

A2 - Collmer, Alan

A2 - Hutcheson, Steven W.

A2 - Mansfield, John W.

A2 - Morris, Cindy E.

A2 - Murillo, Jesus

A2 - Schaad, Norman W.

A2 - Stead, David E.

A2 - Surico, Giuseppe

A2 - Ullrich, Matthias S.

PB - Springer

CY - Dordrecht

ER -

Menestrina G, Coraiola M, Fogliano V, Fiore A, Grgurina I, Carpaneto A et al. Antimicrobial lipodepsipeptides from Pseudomonas spp: a comparison of their activity on model membranes. In Iacobellis NS, Collmer A, Hutcheson SW, Mansfield JW, Morris CE, Murillo J, Schaad NW, Stead DE, Surico G, Ullrich MS, editors, Pseudomonas syringae and related pathogens: biology and genetic. Dordrecht: Springer. 2003. p. 185-198 https://doi.org/10.1007/978-94-017-0133-4_20