Abstract
The structural properties of the Ascaris suum antibacterial factor (ASABF)-type antimicrobial peptides, isolated from nematodes, were compared with the CSαβ-type antimicrobial peptides found in other organisms. The spacing of the half-cystine residues, cysteine pairings, and organization of the precursor were different from the ‘classical’ CSαβ-type antimicrobial peptides, such as drosomycin and plant defensins, and identical only to the MGD and myticin in mollusks. In addition, ABF-5, a member of the ASABF-type antimicrobial peptides in Caenorhabditis elegans, is predicted to contain a basic mature region and an acidic pro-region, similar to MGD and myticin. These results suggest that the ASABF-type antimicrobial peptides, MGD and myticin are similar in their structure.
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