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• W2149502812 startingPage "354" @default.
• W2149502812 abstract "Juvenile hormone esterase (JHE), a member of the carboxylesterase family (EC 3.1.1.1), metabolizes JH that is found in juvenile insects. A highly conserved amphipathic alpha helix is found on the surface of known JHEs. This helix is implicated in receptor-mediated binding and endocytosis of JHE by the pericardial cells resulting in the clearance of JHE activity from the hemolymph. In this study, Lys-204 and Arg-208 of the amphipathic alpha helix of the JHE of Manduca sexta (MsJHE) were mutated to histidine residues generating MsJHE-HH. Pharmacokinetic studies following the injection of MsJHE-HH into the hemocoel of larval M. sexta, Heliothis virescens, and Agrotis ipsilon indicated that MsJHE-HH and wild type MsJHE are cleared at similar rates. The infectivity (lethal concentration and lethal time) of a recombinant baculovirus, AcMsJHE-HH, expressing MsJHE-HH was not significantly different than that of a recombinant baculovirus, AcMsJHE, expressing MsJHE in first instars of H. virescens and A. ipsilon. However, the mass of AcMsJHE-HH-infected larvae was 40–50% lower than that of larvae infected with AcMsJHE, and 70–90% lower than that of wild type AcMNPV-infected larvae." @default.
• W2149502812 created "2016-06-24" @default.
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• W2149502812 date "2011-09-01" @default.
• W2149502812 modified "2023-09-27" @default.
• W2149502812 title "Improved insecticidal efficacy of a recombinant baculovirus expressing mutated JH esterase from Manduca sexta" @default.
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• W2149502812 doi "https://doi.org/10.1016/j.biocontrol.2011.06.002" @default.
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