IDENTIFICATION OF A SEX-PHEROMONE FROM A ROTIFER

The first isolation and characterization of a sex pheromone from a zooplankter is reported. A 29 kdalton glycoprotein on the surface of females of the marine rotifer Brachionus plicatilis acts as a contact-mating pheromone. This glycoprotein (gp29) is glycosylated with oligosaccharides containing N-acetylglucosamine, mannose, and fucose residues, and these oligosaccharides are necessary for male recognition of females. Males detect this signal by contact chemoreception with receptors located in their corona. Binding of purified glycoprotein to male receptors reduces mating attempts by 93%. An antibody to the glycoprotein binds to females, reducing male mating attempts by 86%. When purified gp29 is bound to sepharose beads, it is sufficient to elicit male mating behavior. This glycoprotein is likely to play a key role in the evolution and maintenance of reproductive isolation in rotifers.