title: The baculovirus uses a captured host phosphatase to induce enhanced locomotory activity in host caterpillars.
abstract: The baculovirus is a classic example of a parasite that alters the behavior or physiology of its host so that progeny transmission is maximized. Baculoviruses do this by inducing enhanced locomotory activity (ELA) that causes the host caterpillars to climb to the upper foliage of plants. We previously reported that this behavior is not induced in silkworms that are infected with a mutant baculovirus lacking its protein tyrosine phosphatase (ptp) gene, a gene likely captured from an ancestral host. Here we show that the product of the ptp gene, PTP, associates with baculovirus ORF1629 as a virion structural protein, but surprisingly phosphatase activity associated with PTP was not required for the induction of ELA. Interestingly, the ptp knockout baculovirus showed significantly reduced infectivity of larval brain tissues. Collectively, we show that the modern baculovirus uses the host-derived phosphatase to establish adequate infection for ELA as a virion-associated structural protein rather than as an enzyme.
authors.affiliation: Department of Agricultural and Environmental Biology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo, Japan. katsuma@ss.ab.a.u-tokyo.ac.jp
authors.forename: Susumu
authors.initials: S
authors.lastname: Katsuma
authors.forename: Yasue
authors.initials: Y
authors.lastname: Koyano
authors.forename: Wonkyung
authors.initials: W
authors.lastname: Kang
authors.forename: Ryuhei
authors.initials: R
authors.lastname: Kokusho
authors.forename: Shizuo George
authors.initials: SG
authors.lastname: Kamita
authors.forename: Toru
authors.initials: T
authors.lastname: Shimada
mesh_terms: D000818:Animals; D016367:Baculoviridae / Q000201:enzymology* / Q000235:genetics; D012831:Bombyx / Q000201:enzymology* / Q000235:genetics / Q000821:virology*; D055785:Gene Knockdown Techniques; D019476:Insect Proteins / Q000235:genetics / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D019476:Insect Proteins; D014764:Viral Proteins; D010744:Phosphoric Monoester Hydrolases