Midgut and viral associated proteases of Heliothis armigera.
The role played by the gut juice of insects in the infective process of insect viruses was examined. Analysis of larval gut extract of Heliothis armigera by SDS-PAGE revealed protease activity associated with components of molecular weights 48,000 and 94,000. Proteases were found to be associated with occlusion bodies and virions of both nuclear polyhedrosis virus (NPV) and cytoplasmic polyhedrosis virus (CPV) infecting H. armigera. CPV occlusion bodies were dissolved by gut juice extract at pH 8.0, trypsin and chymotrypsin at pH 8.0, and carbonate-chloride solution at pH 10.5. Trypsin treatment was selective for occlusion bodies of CPV at pH 8.0, whereas solutions more alkaline than pH 10.0 without added enzymes were adequate to digest NPV occlusion bodies. This property was used to identify and separate the two types of viruses from a mixed infection. Gut extract proteases have characteristics similar to those of trypsin.
D000818:Animals; D004064:Digestive System / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007181:Inclusion Bodies, Viral / Q000201:enzymology*; D007304:Insect Viruses / Q000201:enzymology*; D007915:Lepidoptera / Q000382:microbiology*; D008970:Molecular Weight; D009036:Moths / Q000201:enzymology / Q000382:microbiology*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D010447:Peptide Hydrolases; D014357:Trypsin