A hemolytic peptide from the mycophilic fungus Sepedonium chrysospermum (Bull.) Fr |
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| Authors: | Sanguineti Elisa Cosulich Maria E Salis Annalisa Damonte Gianluca Mariotti Mauro G Zotti Mirca |
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| Affiliation: | (1) Mycology Laboratory, Department for the Study of Territory and its Resources (DIP.TE.RIS), Polo Botanico “Hanbury”, University of Genoa, Corso Dogali 1M Genoa, 16136 Genoa, Italy;(2) Department of Biochemistry “A. Castellani”, University of Pavia, Pavia, Italy;(3) Center of Excellence for Biomedical Research (CEBR), University of Genoa, Genoa, Italy |
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| Abstract: | The hemolytic activity of an extract of the mycoparasite Sepedonium chrysospermum (teleomorph Hypomyces chrysospermus) was detected and characterized. Extraction of the fungal biomass by methanol yielded a fraction in which the hemolytic activity against human red blood cells corresponded to a peptide with a molecular mass of 7,653.72 Da and an isoelectric point of approximately 5.8. The peptide was temperature resistant, and the hemolysis was only partially inhibited, even after a 30-min pre-incubation at 100°C. Its hemolytic activity was unaffected by treatment with proteolytic enzymes such as trypsin. Among the divalent cations assayed, Hg2+ was the strongest inhibitor of hemolysis. The reducing agent, dithiothreitol, and the membrane lipid, cholesterol, demonstrated concentration-dependent inhibitory activities. Finally, hemolytic activity triggered by the peptide was analyzed by scanning electron microscopy, and a pore-forming activity was detected. |
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