Improved insecticidal efficacy of a recombinant baculovirus expressing mutated JH esterase from Manduca sexta

El Sayed A El-Sheikh, Shizuo G. Kamita, Kiem Vu, Bruce D. Hammock

Research output: Contribution to journalArticle

16 Scopus citations


Juvenile hormone esterase (JHE), a member of the carboxylesterase family (EC, 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.

Original languageEnglish (US)
Pages (from-to)354-361
Number of pages8
JournalBiological Control
Issue number3
StatePublished - Sep 2011



  • Baculovirus
  • JH
  • JHE
  • Juvenile hormone esterase

ASJC Scopus subject areas

  • Agronomy and Crop Science
  • Insect Science

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