title: Insecticidal activity of two proteases against Spodoptera frugiperda larvae infected with recombinant baculoviruses.
abstract: BACKGROUND
  Baculovirus comprise the largest group of insect viruses most studied worldwide, mainly because they efficiently kill agricultural insect pests. In this study, two recombinant baculoviruses containing the ScathL gene from Sarcophaga peregrina (vSynScathL), and the Keratinase gene from the fungus Aspergillus fumigatus (vSynKerat), were constructed, and their insecticidal properties analysed against Spodoptera frugiperda larvae.
  
  
  RESULTS
  Bioassays of third-instar and neonate S. frugiperda larvae with vSynScathL and vSynKerat showed a decrease in the time needed to kill the infected insects when compared to the wild type virus. We have also shown that both recombinants were able to increase phenoloxidase activity in the hemolymph of S. frugiperda larvae. The expression of proteases in infected larvae resulted in destruction of internal tissues late in infection, which could be the reason for the increased viral speed of kill.
  
  
  CONCLUSIONS
  Baculoviruses and their recombinant forms constitute viable alternatives to chemical insecticides. Recombinant baculoviruses containing protease genes can be added to the list of engineered baculoviruses with great potential to be used in integrated pest management programs.
authors.affiliation: Cell Biology Department, University of Brasília, Brasília, DF, CEP 70910-970, Brazil.
authors.forename: Aline Welzel
authors.initials: AW
authors.lastname: Gramkow
authors.forename: Simone
authors.initials: S
authors.lastname: Perecmanis
authors.forename: Raul Lima Barbosa
authors.initials: RL
authors.lastname: Sousa
authors.forename: Eliane Ferreira
authors.initials: EF
authors.lastname: Noronha
authors.forename: Carlos Roberto
authors.initials: CR
authors.lastname: Felix
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Nagata
authors.forename: Bergmann Morais
authors.initials: BM
authors.lastname: Ribeiro
mesh_terms: D000818:Animals; D001232:Aspergillus fumigatus / Q000201:enzymology; D056668:Cathepsin L / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D002460:Cell Line; D004175:Diptera / Q000201:enzymology; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D005818:Genetic Engineering; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D007306:Insecticides / Q000378:metabolism / Q000494:pharmacology*; D007814:Larva / Q000187:drug effects / Q000821:virology; D017924:Nucleopolyhedroviruses / Q000235:genetics* / Q000502:physiology; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology*; D010572:Pest Control, Biological / Q000379:methods*; D018411:Spodoptera / Q000187:drug effects / Q000254:growth & development / Q000821:virology*
chemical_list: D005656:Fungal Proteins; D019476:Insect Proteins; D007306:Insecticides; D010447:Peptide Hydrolases; C035855:keratinase; D056668:Cathepsin L