title: Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.
abstract: Immune challenge to the insect Podisus maculiventris induces synthesis of a 21-residue peptide with sequence homology to frog skin antimicrobial peptides of the brevinin family. The insect and frog peptides have in common a C-terminally located disulfide bridge delineating a cationic loop. The peptide is bactericidal and fungicidal, exhibiting the largest antimicrobial spectrum observed so far for an insect defense peptide. An all-D-enantiomer is nearly inactive against Gram-negative bacteria and some Gram-positive strains but is fully active against fungi and other Gram-positive bacteria, suggesting that more than one mechanism accounts for the antimicrobial activity of this peptide. Studies with truncated synthetic isoforms underline the role of the C-terminal loop and flanking residues for the activity of this molecule for which we propose the name thanatin.
authors.affiliation: Unité Propre de Recherche 9022, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
authors.forename: P
authors.initials: P
authors.lastname: Fehlbaum
authors.forename: P
authors.initials: P
authors.lastname: Bulet
authors.forename: S
authors.initials: S
authors.lastname: Chernysh
authors.forename: J P
authors.initials: JP
authors.lastname: Briand
authors.forename: J P
authors.initials: JP
authors.lastname: Roussel
authors.forename: L
authors.initials: L
authors.lastname: Letellier
authors.forename: C
authors.initials: C
authors.lastname: Hetru
authors.forename: J A
authors.initials: JA
authors.lastname: Hoffmann
mesh_terms: D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D005658:Fungi / Q000187:drug effects; D006090:Gram-Negative Bacteria / Q000187:drug effects; D006094:Gram-Positive Bacteria / Q000187:drug effects; D006430:Hemiptera; D013058:Mass Spectrometry; D008826:Microbial Sensitivity Tests; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D011898:Ranidae; D017386:Sequence Homology, Amino Acid; D012867:Skin; D013329:Structure-Activity Relationship
chemical_list: D029845:Amphibian Proteins; D000900:Anti-Bacterial Agents; D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; D010456:Peptides, Cyclic; C098076:thanatin; C078413:brevinin-1 protein, Rana