Two novel antimicrobial peptides, which we propose to name termicin and spinigerin, have been isolated from the fungus-growing termite Pseudacanthotermes spiniger (heterometabole insect, Isoptera). Termicin is a 36-amino acid residue antifungal peptide, with six cysteines arranged in a disulfide array similar to that of insect defensins. In contrast to most insect defensins, termicin is C-terminally amidated. Spinigerin consists of 25 amino acids and is devoid of cysteines. It is active against bacteria and fungi. Termicin and spinigerin show no obvious sequence similarities with other peptides. Termicin is constitutively present in hemocyte granules and in salivary glands. The presence of termicin and spinigerin in unchallenged termites contrasts with observations in evolutionary recent insects or insects undergoing complete metamorphosis, in which antimicrobial peptides are induced in the fat body and released into the hemolymph after septic injury.The termite species Pseudacanthotermes spiniger, like the other members of the Macrotermitinae, depends for its nutrition on a symbiotic fungus of the basidiomycete genus Termitomyces (1). This fungus grows inside the nests of the termites on piles of fecal pellets; it predigests the lignocellulosic substances and is responsible for food supply in cellulases. Macrotermitinae also live in symbiosis with anaerobic bacteria present in their posterior gut, which are in part responsible for the complete digestion of cellulose. In this environment inhabited with microorganisms, how do termites protect themselves?The first line of defense of insects against pathogens is the cuticle. Once this barrier has been breached, their defense reactions rely both on cellular and humoral mechanisms. The cellular aspects include phagocytosis and encapsulation of invading microorganisms (for a review, see Ref.2). The humoral facet involves the activation of proteolytic cascades leading to melanization and coagulation. In the evolutionary recent insect orders, the best characterized aspect of the humoral immune response is the rapid synthesis of antimicrobial peptides/ polypeptides by the fat body and certain blood cells and release of these factors into the hemolymph after bacterial challenge. Since the first report of an inducible antibacterial peptide from an insect, cecropin from the moth Hyalophora cecropia (3), more than 200 antimicrobial peptides/polypeptides have been characterized in insects. On the basis of their structural features, the peptides are classified into three classes: (i) linear peptides, devoid of cysteines and forming ␣-helices (the prototype of this family are the insect cecropins (4)), (ii) peptides with an overrepresentation in proline and/or glycine residues, and (iii) open-ended cyclic peptides containing cysteine residues (5). Cecropins, proline-rich, and glycine-rich peptides are essentially active against Gram-negative cells, but their activity spectrum sometimes includes Gram-positive bacteria as targets (6). Two recent reports have also indicated that c...
In response to an experimental infection, the lepidopteran Heliothis virescens produces an antifungal protein named heliomicin. Heliomicin displays sequence similarities with antifungal plant defensins and antibacterial or antifungal insect defensins. To gain information about the structural elements required for either antifungal or antibacterial activity, heliomicin and selected point-mutated variants were expressed in yeast as fusion proteins. The effects of mutations, defined by comparing the primary structure of heliomicin with the sequences of members of the insect defensin family, were analyzed using antibacterial and antifungal assays. One of the variants shows significant activity against Gram-positive bacteria while remaining efficient against fungi. The three-dimensional structures of this variant and of the wild-type protein were determined by two-dimensional (1)H NMR to establish a correlation between structure and antibacterial or antifungal activity. Wild-type and mutated heliomicins adopt a similar scaffold, including the so-called cysteine-stabilized alphabeta motif. A comparison of their structures with other defensin-type molecules indicates that common hydrophobic characteristics can be assigned to all the antifungal proteins. A comparative analysis of various structural features of heliomicin mutant and of antibacterial defensins enables common properties to be assessed, which will help to design new mutants with increased antibacterial activity.
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