Purification and cDNA cloning of a cecropin from the longicorn beetle, Acalolepta luxuriosa.

We have cloned and characterized a novel antibacterial peptide from the hemolymph of the coleopteran insect Acalolepta luxuriosa, of the superfamily Cerambyocidea. This peptide is active against Micrococcus luteus and Escherichia coli, and the amino acid sequence deduced by cloning of the cDNA identifies it as a coleopteran cecropin. Sequence comparisons and phylogenetic analyses performed using Clustal X suggest that this cecropin is evolutionarily intermediate between dipteran and lepidopteran cecropins. The results of MALDI-TOF mass spectrometry indicate that the mature form of this antibacterial peptide is 35 amino acid residues in length and has an amidated C-terminal isoleucine. This report is the first description of a cecropin from a coleopteran insect.