1994 Volume 116 Issue 1 Pages 53-58
Antibacterial activity was induced in the hemolymph of larvae of the coleopteran Tenebrio molitor by injection of Escherichia coli. An antibacterial protein, named tenecin 1, was purified to homogeneity from the larval hemolymph and characterized. A cDNA clone for tenecin 1 was isolated and its complete sequence was determined. This protein was found to inhibit the growth of Gram-positive bacteria and to consist of 43-amino acid residues including six cysteine residues. The disulfide structure of tenecin 1 was determined by sequencing cysteine containing peptides obtained by digesting tenecin 1 with endopeptidase Lys-C, trypsin, and thermolysin. The amino acid sequence and its disulfide bonds were similar to those of sapecin and sapecin C, antibacterial proteins of Sarcophaga peregrina.
