A hemolytic peptide from the mycophilic fungus Sepedonium chrysospermum (Bull.) Fr.
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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.
KeywordsMycoparasite Hemolysis Sepedonium chrysospermum Peptide
We are grateful to Hugo Monaco, Paolo Davoli, and Nicola Sitta for the critical reading of the manuscript and helpful suggestions. We thank Cristina Bernini, CNR-Spin, for performing SEM analysis. Research performed towards the Ph.D. in Botany Applied to Agriculture and Environment (University of Genoa, DIPTERIS) was supported by the Ministry of Education, University and Research, by the “Fund for support of youth” (DM 23.10.2003, no. 198), and was devoted to the priority area 9 (Enhancement of typical food and agriculture products and food safety through new methods of characterization and quality assurance).
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