Purification and cDNA cloning of luxuriosin, a novel antibacterial peptide with Kunitz domain from the longicorn beetle, Acalolepta luxuriosa.
We have purified a novel antibacterial peptide from the hemolymph of the coleopteran insect Acalolepta luxuriosa, of the family Cerambyocidae, and named it luxuriosin. This peptide showed growth-inhibitory activity against Micrococcus luteus and germination- and/or growth-inhibitory activity against the conidia from rice blast fungus, Magnaporthe grisea. The amino acid sequence determined by cDNA cloning identified luxuriosin as a peptide of 88 amino acids with a theoretical molecular weight of 10,368.34, containing a Kunitz domain.
Ueda
Kenjiro
K
Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Naka-cho 2-24-16, Koganei, Tokyo 184-8588, Japan.
Saito
Ayaka
A
Imamura
Morikazu
M
Miura
Nami
N
Atsumi
Shogo
S
Tabunoki
Hiroko
H
Watanabe
Ayako
A
Kitami
Madoka
M
Sato
Ryoichi
R
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D001517:Coleoptera; D006458:Hemolymph / Q000737:chemistry; D006801:Humans; D019476:Insect Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D012689:Sequence Homology, Nucleic Acid
D023181:Antimicrobial Cationic Peptides; D019476:Insect Proteins