Paper Report for: Temeyer_2013_Pestic.Biochem.Physiol_106_118
Reference
Title: Acetylcholinesterase of Rhipicephalus (Boophilus) microplus and Phlebotomus papatasi: Gene identification, expression, and biochemical properties of recombinant proteins Temeyer KB, Olafson PU, Brake DK, Tuckow AP, Li AY, Perez de Leon AA Ref: Pesticide Biochemistry and Physiology, 106:118, 2013 : PubMed
The southern cattle tick Rhipicephalus (Boophilus) microplus (Bm) is a vector of bovine babesiosis and anaplasmosis. Tick resistance to organophosphate (OP) acaricide involves acetylcholinesterase (AChE) insensitivity to OP and metabolic detoxification. Sequencing and in vitro expression of Bm genes encoding AChE allowed biochemical characterization of three BmAChEs expressed in tick synganglion. rBmAChE1, rBmAChE2 and rBmAChE3 exhibited substrate preference for acetylthiocholine, high substrate inhibition and sensitivity to AChE-specific inhibitors. OP-insensitivity mutations were demonstrated in rBmAChE1 and rBmAChE3. Gene silencing suggested functional complementation of BmAChEs in vivo. BmAChE genes were amplified in copy number and multiple transcript polymorphisms were expressed in individual tick synganglia for each of the BmAChEs, suggesting allelic diversity within individuals. Studies also identified a gene encoding AChE of the sand fly, Phlebotomus papatasi, a vector of leishmaniasis in humans and animals. Expression of recombinant P. papatasi AChE (rPpAChE) enabled biochemical characterization and identification of effective inhibitors that selectively target rPpAChE.
Temeyer KB, Olafson PU, Brake DK, Tuckow AP, Li AY, Perez de Leon AA (2013) Acetylcholinesterase of Rhipicephalus (Boophilus) microplus and Phlebotomus papatasi: Gene identification, expression, and biochemical properties of recombinant proteins Pesticide Biochemistry and Physiology106: 118-123
Temeyer KB, Olafson PU, Brake DK, Tuckow AP, Li AY, Perez de Leon AA (2013) Pesticide Biochemistry and Physiology106: 118-123