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The Interaction of Lipodepsipeptide Toxins from Pseudomonas syringae pv. syringae with Biological and Model Membranes: A Comparison of Syringotoxin, Syringomycin, and Two Syringopeptins

May 1999 , Volume 12 , Number  5
Pages  391 - 400

Mauro Dalla Serra , 1 Giulia Fagiuoli , 1 Paola Nordera , 1 Ivonne Bernhart , 1 Claudio Della Volpe , 2 Domenico Di Giorgio , 3 Alessandro Ballio , 3 and Gianfranco Menestrina 1

1CNR-ITC Centro Fisica Stati Aggregati, Via Sommarive 18, I-38050 Povo (Trento), Italy; 2Dipartimento di Ingegneria dei Materiali, Università di Trento, Via Mesiano 77, I-38050 Mesiano (Trento), Italy; 3Dipartimento di Scienze Biochimiche e Centro CNR di Biologia Molecolare, Roma “La Sapienza,” P.le Aldo Moro 5, 00185 Roma, Italy

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Accepted 22 January 1999.

Pseudomonas syringae pv. syringae produces two groups of cyclic lipodepsipeptides (LDPs): the nona-peptides syringomycins, syringostatins, and syringotoxin (ST), and the more complex syringopeptins composed of either 22 or 25 amino acid residues (SP22 and SP25). Both classes of peptides significantly contribute to bacterial pathogenesis and their primary target of action seems to be the plasma membrane. We studied and compared the activity of some members of these two classes of LDPs on red blood cells and on model membranes (monolayers and unilamellar vesicles). All peptides induced red blood cell hemolysis. The mechanism was apparently that of a colloid-osmotic shock caused by the formation of pores, as it could be prevented by osmoticants of adequate size. Application of the Renkin equation indicated a radius of approximately 1 nm for the lesions formed by syringopeptins SP22A and SP25A, whereas those formed by syringomycin E (SRE) had a variable, dose-dependent size ranging from 0.7 up to 1.7 nm. All tested LDPs displayed surface activity, forming peptide monolayers with average molecular areas of 1.2 nm2 (SRE), 1.5 nm2 (SP22A), and 1.3 nm2 (SP25A). They also partitioned into preformed lipid monolayers occupying molecular areas that ranged from 0.6 to 1.7 nm2 depending on the peptide and the lipid composition of the film. These LDPs formed channels in lipid vesicles as indicated by the release of an entrapped fluorescent dye (calcein). The extent of permeabilization was dependent on the concentration of the peptide and the composition of the lipid vesicles, with a preference for those containing a sterol. From the dose dependence of the permeabilization it was inferred that LDPs increased membrane permeability by forming oligomeric channels containing from four to seven monomers. On average, syringopeptin oligomers were smaller than SRE and ST oligomers.

Additional keywords: calcein release, detergents, lipid bilayer.

© 1999 The American Phytopathological Society