title: A melittin-related peptide from the skin of the Japanese frog, Rana tagoi, with antimicrobial and cytolytic properties.
abstract: Two peptides with antimicrobial and cytolytic properties were purified from an extract of the skin of Tago's brown frog Rana tagoi. The primary structure of one peptide (FLPILGKLLS(10)GIL.NH(2)) identifies it as a member of the temporin family, whereas the second peptide (AIGSILGALA(10)KGLPTLISWI(20)KNR.NH(2)) displays 78% sequence identity to melittin from the venom of the honeybee Apis florea. Compared with melittin, the melittin-related peptide (MRP) was equipotent in inhibiting the growth of the Gram-positive bacterium Staphylococcus aureus, 5-fold less potent against the Gram-negative bacterium Escherichia coli and against the fungal pathogen, Candida albicans. MRP was 13-fold less hemolytic than melittin against human erythrocytes and 4- and 5-fold less cytolytic against mouse EL4 T-lymphoma-derived cells and L929 fibroblasts, respectively. However, at non-cytotoxic concentrations (<or=8 microM), MRP did not protect HeLa cells from cell death produced by human rhinovirus type 2 infection.
authors.affiliation: Department of Biochemistry, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al-Ain 17666, United Arab Emirates. jmconlon@uaeu.ac.ae
authors.forename: J Michael
authors.initials: JM
authors.lastname: Conlon
authors.forename: Agnes
authors.initials: A
authors.lastname: Sonnevend
authors.forename: Mahendra
authors.initials: M
authors.lastname: Patel
authors.forename: Vijayayasarathy
authors.initials: V
authors.lastname: Camasamudram
authors.forename: Norbert
authors.initials: N
authors.lastname: Nowotny
authors.forename: Erika
authors.initials: E
authors.lastname: Zilahi
authors.forename: Shawichi
authors.initials: S
authors.lastname: Iwamuro
authors.forename: Per F
authors.initials: PF
authors.lastname: Nielsen
authors.forename: Tibor
authors.initials: T
authors.lastname: Pál
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins / Q000737:chemistry* / Q000502:physiology; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D000998:Antiviral Agents / Q000494:pharmacology; D002460:Cell Line; D004926:Escherichia coli / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008555:Melitten / Q000737:chemistry; D051379:Mice; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000502:physiology; D011898:Ranidae; D017386:Sequence Homology, Amino Acid; D012867:Skin / Q000378:metabolism; D013997:Time Factors
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D000998:Antiviral Agents; D010455:Peptides; D011506:Proteins; C475804:melittin-related peptide, Rana tagoi; C514607:temporin-1TGa, Rana tagoi; D008555:Melitten