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.
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http://dx.doi.org/10.1016/j.bbagen.2004.11.014 | DOI Listing |
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