title: Functional mapping of amino acid residues responsible for the antibacterial action of apidaecin.
abstract: Functional mapping was carried out to address the amino acid residues responsible for the activity of the antibacterial peptide apidaecin from the honeybee by an in vivo assay system developed previously. The C-terminal region and many of the proline and arginine residues which are present at high frequency in apidaecin were found to play an important role in its antibacterial activity.
authors.affiliation: Department of Biological Science and Technology, Science University of Tokyo, Chiba, Japan. staguchi@rs.noda.sut.ac.jp
authors.forename: S
authors.initials: S
authors.lastname: Taguchi
authors.forename: A
authors.initials: A
authors.lastname: Ozaki
authors.forename: K
authors.initials: K
authors.lastname: Nakagawa
authors.forename: H
authors.initials: H
authors.lastname: Momose
mesh_terms: D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D001483:Base Sequence; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000235:genetics / Q000494:pharmacology*; D013329:Structure-Activity Relationship
chemical_list: D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C061361:apidaecin