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Vol. 273, Issue 4, 2059-2066, January 23, 1998

Lycotoxins, Antimicrobial Peptides from Venom of the Wolf Spider Lycosa carolinensis

From the Environmental Toxicology Graduate Program and the Department of Entomology, University of California, Riverside, California 92521

Two peptide toxins with antimicrobial activity, lycotoxins I and II, were identified from venom of the wolf spider Lycosa carolinensis (Araneae: Lycosidae) by virtue of their abilities to reduce ion and voltage gradients across membranes. Both peptides were purified to homogeneity by reversed-phase liquid chromatography and determined to have the following primary structures by Edman microsequencing: IWLTALKFLGKHAAKHLAKQQLSKL-NH₂ for lycotoxin I and KIKWFKTMKSIAKFIAKEQMKKHLGGE-OH for lycotoxin II. The predicted secondary structures of the lycotoxins display amphipathic -helix character typical of antimicrobial pore-forming peptides. Antimicrobial assays showed that both lycotoxins potently inhibit the growth of bacteria (Escherichia coli) and yeast (Candida glabrata) at micromolar concentrations. To verify its hypothesized pore-forming activity, lycotoxin I was synthesized and shown to promote efflux of Ca²⁺ from synaptosomes, to cause hemolysis of erythrocytes, and to dissipate voltage gradients across muscle membrane. The lycotoxins may play a dual role in spider-prey interaction, functioning both in the prey capture strategy as well as to protect the spider from potentially infectious organisms arising from prey ingestion. Spider venoms may represent a potentially new source of novel antimicrobial agents with important medical implications.

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