Journal
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
Volume 142, Issue 3, Pages 317-323Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpb.2005.08.001
Keywords
cecropin; antibacterial peptide; purification; Coleoptera; insect immunity; Acalolepta luxuriosa; hemolymph; MALDI-TOF
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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. (c) 2005 Elsevier Inc. All rights reserved.
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