Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae.
Hinnavins, together with lysozymes, are the main types of antibacterial peptides/proteins previously isolated from the larval haemolymph of the cabbage butterfly, Artogeia rapae as part of the humoral immune response to a bacterial invasion. One of these antibacterial peptides, named hinnavin II, was purified and characterized after cDNA cloning. The purified hinnavin II was more active against Gram negative than against Gram positive bacteria. Hinnavin II also showed a powerful synergistic effect on the inhibition of bacterial growth with purified lysozyme. The cDNA has a total length of 186 bp with a 114 coding region. The deduced protein sequence contains 38 amino acids with a coding capacity of 4142.8 Da. The result of a multiple sequence alignment and phylogenetic analysis with Clustal W indicated that mature hinnavin II showed an approximately 78.9% amino acid sequence identity with cecropin A and originated from a group containing mostly lepidopteran cecropins.
Yoe
Sung Moon
SM
Department of Biological Sciences, Dankook University, Cheonan 330-714, South Korea.
Kang
Chang Soo
CS
Han
Sung Sik
SS
Bang
In Seok
IS
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000819:agonists / Q000235:genetics* / Q000302:isolation & purification*; D001483:Base Sequence; D002080:Butterflies / Q000235:genetics* / Q000254:growth & development; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry; D007814:Larva / Q000235:genetics; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D019476:Insect Proteins; C108747:hinnavin I protein, Artogeia rapae; C031161:cecropin A; D009113:Muramidase