HINNAVIN-I, AN ANTIBACTERIAL PEPTIDE FROM CABBAGE BUTTERFLY, ARTOGEIA-RAPAE

We have previously isolated four antibacterial peptides from the immun e haemolymph of the fifth instar larvae of cabbage butterfly, Artogeia rapae [Yoe, S. M., Bang, I. S., Kang, C. S., and Kim, H. J. (1996) Mo l. Cells 6, 609-614]. They were induced by live, nonpathogenic Gram ne gative bacteria. One of these novel antibacterial peptides was named h innavin I. Hinnavin I is heat stable; its activity was retained after 60 min incubation at 100 degrees C, being effective against Gram negat ive and/or Gram positive bacteria. Hinnavin I and lysozyme II showed a powerful synergistic effect on the inhibition of bacterial growth. Am ino acid composition was analyzed and the molecular weight was determi ned to be 4,139.94 +/- 10.91 Da by the ESI mass spectrometer. To eluci date the primary structure of hinnavin I, the amino acid sequence of t his peptide was determined by N-terminal sequencing techniques. The am ino-terminal half of the molecule was rich in charged amino acids and was hydrophilic, whereas the carboxyl-terminal half was hydrophobic.