Abstract

Almost all Lepidoptera produce two kinds of spermatozoa, a typical nucleated spermatozoön and an anucleate one. Inactive in the male prior to ejaculation, both of these spermatozoa become motile upon ejaculation and move to the female's sperm storage organ. This study shows that in several phylogenetically and morphologically diverse species of Lepidoptera, the anucleate spermatozoa, or parasperm (also known as apyrene spermatozoa), and the nucleated spermatozoa, or eusperm (also known as eupyrene spermatozoa), are activated by a protein of approximately 37.7 kDa added by a secretion from the male. Although proteases have been shown to activate these parasperm, inhibitors of proteases did not prevent activation of the tobacco hornworm moth, Manduca sexta, parasperm, even at well over normal working concentrations of the inhibitors. Parasperm could also be activated by an ionophore, indicating that a trans-membrane ionic event is involved. In contrast to parasperm, eusperm are first ejaculated as bundles of 256 spermatozoa. This study identified a male protein of similar molecular weight that dissociates the eusperm from the bundles, but that is sensitive to proteases. Based on these characteristics, the activators of both types of spermatozoa appear to be different from the initiatorin imputed to be the activator of commercial silkmoth, Bombyx mori, spermatozoa. The role of these proteins in these unique modes of lepidopterous sperm activation may have been adapted from other roles in other kinds of insects, and indicates especially an important function of parasperm in the reproductive physiology and/or behavior of female lepidopterans.

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