Social Wasp Venoms Research Articles

Kinins in ant venoms—A comparison with venoms of related hymenoptera

1. Venom preparations have been made of six ant, one pompilid wasp, two mutillid wasp, and four social wasp species. 2. The venoms were analysed pharmacologically in order to detect kinin-like activity. 3. Due to the small amounts of venoms available only a cascade of smooth muscle preparation could be used. 4. Kinin activities have been found in five ant venoms and in four social wasp venoms. 5. No kinin activity has been found in the venoms of the pompilid and mutillid wasps. 6. All ant venoms also contain unidentified agonists for vertebrate smooth muscle preparations.

Synergistic effects of agonists and antagonists in insect venoms—a natural way of insecticidal action

AbstractContrary to the typical killing action of most animal venoms, including social wasp venoms, the solitary wasp venoms seem to have been created to paralyse the prey. This suggests a specific action on parts of the nervous system. However, the solitary wasp venoms studied, contain many agonists and antagonists of synaptic transmission, and their paralysing action is very complicated. Besides a contribution of agonists to initiate and enhance the action of antagonists, one of the venoms contains two antagonists with different actions, and one of these antagonists enhances the effect of the other. The specific action of both toxins and their interaction will be discussed as an example of how nature enhances pesticide action through mixtures.

Comparative enzymology of venoms from stinging Hymenoptera

J. O. Schmidt, M. S. Blum and W. L. Overal. Comparative enzymology of venoms from stinging Hymenoptera. Toxicon 24, 907 – 921, 1986. — Venoms from 20 species of stinging Hymenoptera, including nine species of ants and nine species of social wasps, were quantitatively analyzed for the following enzymic activities: phospholipase A, hyaluronidase, lipase, esterase, protease, acid phosphatase, alkaline phosphatase and phosphodiesterase. Phospholipase and hyaluronidase were present in all the venoms, with activity levels generally higher among the wasps than the ants ( P < 0.05). Lipase was present in high activity in several social wasp venoms and one ant venom, in low levels in two other ant venoms and absent from four tested snake venoms. Two-carbon esterase activity was present in the venoms of five social wasps and one ant. Non-specific protease was present at very high activity levels in the venoms of an army ant species and was also present in the venoms of a social wasp and another ant. Acid phosphatase activity was present in eight of the nine ant venoms, but was essentially absent from all the social wasp venoms. Alkaline phosphatase activity was clearly detectable in the venoms of only two species of ants. Phosphodiesterase, an enzyme not previously detected in insect venoms, was present in the venoms of three closely related ant species. Venoms with generally high enzymic activities included those of Polistes infuscatus, Vespula ( V.) squamosa and Pogonomyrmex badius; those with low activities included Dolichovespula maculata, Apoica pallens and Dasymutilla lepeletierii. The 20 venoms were ranked according to overall activity levels using the eight enzyme activities plus lethal, hemolytic and pain-inducing activities. They were also compared phylogenetically using these 11 activities.