In this study we measured in vitro honey bee enzyme activities in presence of the synergist piperonyl butoxide (PBO) and some new benzodioxole and dihydrobenzofuran derivatives through absorbance and fluorescence spectrophotometric assays, to determine if and to what extent detoxification systems and acetylcholinesterases are affected by these compounds. Both Italian (Italy) and Carniolan (Czech Republic) honey bees were tested. In the case of Italian honey bees the esterase activity was partially but significantly inhibited by almost all the tested products. In Carniolan honey bees only the dihydrobenzofuran derivative EN16-41 significantly inhibited esterases. Other enzymatic systems, such as cytochrome P450 monooxygenases (P450s) and glutathione S-transferases (GSTs), often involved in xenobiotics detoxification, as well as acetylcholinesterases (AchEs) seem not to be targeted by the studied synergists. These data seem to suggest that some of the investigated PBO analogues could not be detrimental to honey bees.
In vitro study on enzymatic systems of honeybees
Education 1997 - 2004 Faculty of Veterinary Hygine and Ecology - University of Veterinary and Pharmaceutical Sciences Brno Employment 2015 - now - Czech University of Life Sciences Prague 2010 - now - Bee Research Institute Dol - Ltd.; researcher 2004 - 2009 Department of Parasitology; University of Veterinary and Pharmaceutical Sciences Brno; assistant Research interest Bees and host-parasite interactions; host specifity and transmission of parasites; experimental studies under laboratory and field conditions