Properties of a baculovirus mutant defective in the protein phosphatase gene.
Autographa california nuclear polyhedrosis virus (AcMNPV) contains a gene, ptp, encoding a protein tyrosine/serine phosphatase, BV-PTP. To investigate the biological function of ptp in the baculoviral replication cycle, we constructed a recombinant baculovirus, vPTPdel, in which the catalytically active site of BV-PTP was deleted. Although the vPTPdel mutant was viable in cell culture, it was partially defective in occluded virus production in SF-21 but not TN-368 cell lines. SF-21 cells infected with vPTPdel were heterogeneous in their ability to support occluded virus production. These results suggest that BV-PTP functions in a cell line-specific and possibly a cell cycle-specific fashion. The yield of occlusion bodies, infectivity (concentration of virus causing 50% mortality) and virulence (the time at which 50% of the cells died) of vPTPdel appeared to be normal in insect larvae. We identified a 35-kDa phosphoprotein as a potential target of the BV-PTP in SF-21 cells.
Li
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Department of Genetics, University of Georgia, Athens 30602, USA.
Miller
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LK
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D017353:Gene Deletion; D005814:Genes, Viral; D008969:Molecular Sequence Data; D009154:Mutation; D017924:Nucleopolyhedroviruses / Q000235:genetics* / Q000502:physiology; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000235:genetics*; D011506:Proteins / Q000378:metabolism; D018411:Spodoptera; D014774:Virulence; D014779:Virus Replication
D011506:Proteins; D017027:Protein Tyrosine Phosphatases