Baculoviruses encode a conserved sulfhydryl oxidase, Ac92, P33 proteins. Its role during viral replication is unknown but Ac92 has homology to
the family of flavin adenine dinucleotide-linked sulfhydryl oxidases. It is related to the ERV/ALR family of sulfhydryl oxidases, which is necessary
for budded virus (BV) production and multinucleocapsid occlusion-derived virus (ODV) formation. Here, we attempted to supress the protein P33
using molecular docking. The active ingredients of Phyllanthus amarus was used as ligands. Resulted in the successful docking result with high
binding affinity of -10.0 and -9.1 Kcal/Mol for Norsecurinine and Securinine. Along with this, we also deduce the Protein-protein interaction
network using two major proteins such as Putative Baculovirus FP protein and AcMNPV Baculovirus orf 2 Cun001 putative bro proteins. The
networks are clearly showing the function of BmNPV gene depending on other functional proteins.
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