TL;DR: The baculovirus induced a new aphidicolin-sensitive, alpha-like, DNA polymerase upon infection of the lepidopteran noctuid, Trichoplusia ni, which differed in their sensitivities to heat inactivation, high salt concentrations, and 0.1 M phosphate buffer.
Abstract: The baculovirus, Autographa california nuclear polyhedrosis virus, induced a new aphidicolin-sensitive, alpha-like, DNA polymerase upon infection of the lepidopteran noctuid, Trichoplusia ni The new virus-induced DNA polymerase could be separated from the host alpha-like polymerase by phosphocellulose chromatography The two polymerases differed in their sensitivities to heat inactivation, high salt concentrations, and 01 M phosphate buffer
TL;DR: It is suggested that the protein product of the Autographa californica nuclear polyhedrosis virus p143 may function by direct binding to DNA, consistent with the essential role of P143 for viral DNA replication and suggest that P143 may perform other functions at late times after infection.
TL;DR: The doubling time, virus yield, and susceptibility of five lepidopteran cell lines, Trichoplusia ni, Spodoptera frugiperda, Heliothis virescens, Plutella xylostella, and Anticarsia gemmatalis to the Autographa californica multiple nuclear polyhedrosis virus (AcMNPV) were compared.
TL;DR: The cry2Aa and cry2Ab genes from a Brazilian Bacillus thuringiensis strain were introduced into the genome of the baculovirus Autographa californicamultiple nucleopolyhedrovirus (AcMNPV) in order to evaluate the heterologous proteins expression in insect cells and their toxicity to different insects.
Abstract: The cry2Aa and cry2Ab genes from a Brazilian Bacillus thuringiensis strain were introduced into the genome of the baculovirus Autographa californicamultiple nucleopolyhedrovirus (AcMNPV) in order to evaluate the heterologous proteins expression in insect cells and their toxicity to different insects. The recombinant viruses (vAcCry2Aa and vSynCry2Ab) were amplified in Trichoplusia ni (BTI-Tn5B1-4) cells and used to infect Spodoptera frugiperda larvae. Total extracts from S. frugiperda infected with the recombinant viruses were analysed by SDS-PAGE, which detected the presence of polypeptides around 65 kDa. Cuboid-shaped protein crystals were observed in insect extracts by light and scanning electron microscopy. Bioassays, using the heterologous proteins showed toxicity against second instar A. gemmatalis larvae (Cry2Aa) with a LC50 of 1.03 μg/ml and second instar S. frugiperda larvae (Cry2Ab) with a LC50 of 3.45 μg/ml. No toxic activity was detected for Aedes aegypti and Culex quinquenfaciatus.