title: Scarabaecin, a novel cysteine-containing antifungal peptide from the rhinoceros beetle, Oryctes rhinoceros.
abstract: A novel antifungal peptide, scarabaecin (4080Da), was isolated from the coconut rhinoceros beetle, Oryctes rhinoceros. Scarabaecin cDNA was cloned by reverse transcriptase-polymerase chain reactions (RT-PCR) using a primer based on the N-terminal amino acid sequence. The amino acid sequence deduced from scarabaecin cDNA showed no significant similarity to those of reported proteins. Chemically synthesized scarabaecin indicated antifungal activity against phytopathogenic fungi such as Pyricularia oryzae, Rhizoctonia solani, and Botrytis cinerea, but not against phytopathogenic bacteria. It showed weak activity against Bauberia bassiana, an insect pathogenic fungus, and Staphylococcus aureus, a pathogenic bacterium. Scarabaecin showed chitin binding property and its K(d) was 1.315 microM. A comparison of putative chitin-binding domains among scarabaecin, invertebrate, and plant chitin-binding proteins suggests that scarabaecin is a new member of chitin-binding antimicrobial proteins.
authors.affiliation: Biological Research Laboratories, Nissan Chemical Industries, Ltd., Shiraoka, Saitama, Japan.
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Tomie
authors.forename: Jun
authors.initials: J
authors.lastname: Ishibashi
authors.forename: Seiichi
authors.initials: S
authors.lastname: Furukawa
authors.forename: Satoe
authors.initials: S
authors.lastname: Kobayashi
authors.forename: Ryoko
authors.initials: R
authors.lastname: Sawahata
authors.forename: Ai
authors.initials: A
authors.lastname: Asaoka
authors.forename: Michito
authors.initials: M
authors.lastname: Tagawa
authors.forename: Minoru
authors.initials: M
authors.lastname: Yamakawa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D001483:Base Sequence; D003001:Cloning, Molecular; D001517:Coleoptera / Q000737:chemistry*; D005658:Fungi / Q000187:drug effects; D019476:Insect Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000235:genetics; D016415:Sequence Alignment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins; D010940:Plant Proteins; C476450:scarabaecin protein, Oryctes rhinoceros