title: Impact of a basement membrane-degrading protease on dissemination and secondary infection of Autographa californica multiple nucleopolyhedrovirus in Heliothis virescens (Fabricus).
abstract: ScathL is a cathepsin L-like cysteine protease from the flesh fly, Sarcophaga peregrina, that digests components of the basement membrane (BM) during insect metamorphosis. A recombinant baculovirus that expresses ScathL (AcMLF9.ScathL) kills larvae of the tobacco budworm, Heliothis virescens, significantly faster than the wild-type virus and triggers melanization and tissue fragmentation in infected larvae shortly before death. As BMs are a potential barrier to the spread of baculovirus secondary infection to other tissues in the host, this study tested the hypothesis that the rapid death of insects infected with AcMLF9.ScathL was caused by accelerated secondary infection resulting from the degradation of host BMs by ScathL. Viruses expressing catalytically active or inactive ScathL were used to examine the effects of ScathL activity on budded virus release into the haemocoel during infection, the production of polyhedra in infected larvae and the rate of infection of the gut, trachea, haemocytes, fat body and Malpighian tubules. It was concluded that the enhanced insecticidal efficacy of the recombinant baculovirus that expresses ScathL does not result from altered tissue tropism or accelerated systemic infection. Implications for the role of the BM as a barrier to baculovirus dissemination within the host insect are discussed.
authors: Department of Entomology, Iowa State University, Ames, IA 50011, USA.
authors: Huarong
authors: H
authors: Li
authors: Department of Entomology, Iowa State University, Ames, IA 50011, USA.
authors: Hailin
authors: H
authors: Tang
authors: Department of Entomology, Iowa State University, Ames, IA 50011, USA.
authors: Robert L
authors: RL
authors: Harrison
authors: Department of Entomology, Iowa State University, Ames, IA 50011, USA.
authors: Bryony C
authors: BC
authors: Bonning
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004064:Digestive System / Q000821:virology; D005216:Fat Body / Q000821:virology; D006434:Hemocytes / Q000821:virology; D006458:Hemolymph / Q000821:virology; D007814:Larva / Q000821:virology; D008317:Malpighian Tubules / Q000821:virology; D009036:Moths / Q000821:virology*; D017924:Nucleopolyhedroviruses / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity / Q000502:physiology*; D014132:Trachea / Q000821:virology
chemical_list: D002403:Cathepsins; D003546:Cysteine Endopeptidases; D056668:Cathepsin L