Baculovirus Replication: Phosphorylation of Polypeptides Synthesized in Trichoplusia ni Nuclear Polyhedrosis Virus-infected Cells

Kelly, D. C.; Lescott, Thelma

doi:10.1099/0022-1317-65-7-1183

Cited by 24 publications

(15 citation statements)

References 10 publications

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“…However, phosphorylation of pp31 appeared to lag slightly behind synthesis, because labeling with 35 S was first detected at 0 to 4 h postinfection whereas labeling with 32 P i was first detected at 4 to 8 h postinfection. Previously, it had been reported that 32 P i -labeled pp31 was detected only in the nuclear fraction (11,18), but we clearly detected phosphorylated pp31 in both the cytosolic and nuclear fractions in this study (Fig. 2B).…”

Section: Time Course Of Pp31 Synthesis and Phosphorylationsupporting

confidence: 50%

Dynamic phosphorylation of Autographa californica nuclear polyhedrosis virus pp31

Broussard

Guarino

Jarvis

1996

J Virol

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Autographa californica nuclear polyhedrosis virus (AcMNPV) pp31 is a nuclear phosphoprotein that accumulates in the virogenic stroma, which is the viral replication center in the infected-cell nucleus, binds to DNA, and serves as a late expression factor. Considering that reversible phosphorylation could influence its functional properties, we examined phosphorylation and dephosphorylation of pp31 in detail. Our results showed that pp31 is posttranslationally phosphorylated by both cellular and virus-encoded or -induced kinases. Threonine phosphorylation of pp31 by the virus-specific kinase activity was sensitive to aphidicolin, indicating that it requires late viral gene expression. We also found that pp31 is dephosphorylated by a virus-encoded or -induced phosphatase(s), indicating that phosphorylation of pp31 is a dynamic process. Analysis of pp31 fusion proteins showed that pp31 contains at least three phosphorylation sites. The amino-terminal 100 amino acids of pp31 include at least one serine residue that is phosphorylated by a cellular kinase(s). The C-terminal 67 amino acids of pp31 include at least one threonine residue that is phosphorylated by the virus-specific kinase(s). Finally, this C-terminal domain of pp31 includes at least one serine that is phosphorylated by either a host or viral kinase(s). Interestingly, site-directed mutagenesis of the consensus threonine phosphorylation sites in the C-terminal domain of pp31 failed to prevent threonine phosphorylation, suggesting that the virus-specific kinase is unique and has an undetermined recognition site.

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Section: Time Course Of Pp31 Synthesis and Phosphorylationsupporting

confidence: 50%

Dynamic phosphorylation of Autographa californica nuclear polyhedrosis virus pp31

Broussard

Guarino

Jarvis

1996

J Virol

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“…Phosphorylation or dephosphorylation is often associated with protein activation or inactivation, respectively. Baculovirus proteins undergo phosphorylation in infected cells (63,64), and multiple phosphoproteins were detected in BV and ODV (12,63,64). A total of 23 baculoviral proteins were identified as phosphoproteins in our study (Table 3).…”

Section: Discussionmentioning

confidence: 94%

Comparative Proteomics Reveal Fundamental Structural and Functional Differences between the Two Progeny Phenotypes of a Baculovirus

Hou

Zhang

Deng

et al. 2013

J Virol

100

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The replication of lepidopteran baculoviruses is characterized by the production of two progeny phenotypes: the occlusion-derived virus (ODV), which establishes infection in midgut cells, and the budded virus (BV), which disseminates infection to different tissues within a susceptible host. To understand the structural, and hence functional, differences between BV and ODV, we employed multiple proteomic methods to reveal the protein compositions and posttranslational modifications of the two phenotypes of Helicoverpa armigera nucleopolyhedrovirus. In addition, Western blotting and quantitative mass spectrometry were used to identify the localization of proteins in the envelope or nucleocapsid fractions. Comparative protein portfolios of BV and ODV showing the distribution of 54 proteins, encompassing the 21 proteins shared by BV and ODV, the 12 BV-specific proteins, and the 21 ODV-specific proteins, were obtained. Among the 11 ODV-specific envelope proteins, 8 either are essential for or contribute to oral infection. Twenty-three phosphorylated and 6 N-glycosylated viral proteins were also identified. While the proteins that are shared by the two phenotypes appear to be important for nucleocapsid assembly and trafficking, the structural and functional differences between the two phenotypes are evidently characterized by the envelope proteins and posttranslational modifications. This comparative proteomics study provides new insight into how BV and ODV are formed and why they function differently. Baculoviruses are insect-specific pathogens containing large circular double-stranded DNA genomes. Over millions of years of interdependence between viruses and their natural insect hosts, both have undergone a coevolution, such that lepidopteran baculoviruses have developed a unique biphasic replication cycle that generates two progeny phenotypes, the budded virus (BV) and the occlusion-derived virus (ODV). ODVs are embedded in occlusion bodies (OBs) that offer the virions a certain amount of protection against environmental degradation. Once ingested by a susceptible insect, ODVs are released from OBs within the larval midgut and initiate oral infection. After infecting midgut epithelial cells, BVs are synthesized and released to disseminate systemic infection of different tissues within the larval host. The two phenotypes have been used in a wide range of applications. Due to their expandable genome and the presence of very strong promoters, BVs have been established as successful vectors for the expression of thousands of proteins and have also been studied as potential vectors for gene therapy (1). The OBs of certain baculoviruses have been widely used in agriculture and forestry as viable alternatives to chemical insecticides in insect pest control (2).The broad applications of baculoviruses provide a strong rationale for identifying the proteins associated with both phenotypes and for understanding their roles in baculovirus infection. While previous proteomic studies have elucidated the protein compositions of a...

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“…Nucleocapsids were purified from detergent-treated virus particles as described by Bur|ey et al (1982). 3:p-radiolabelled CRV was produced as described by Kelly & Lescott (1984).…”

Section: Introductionmentioning

confidence: 99%

Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

Wang

Kelly

1985

Journal of General Virology

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SUMMARYThe uptake of two forms of Trichoplusia ni multiple nucleocapsid nuclear polyhedrosis virus by SpodopleraJrugiperda cells in culture has been evaluated. Subtle differences in the Mg 2+ and Ca 2+ requirements for the uptake of cell-released virus (CRV) and polyhedron-derived virus (PDV) exist; otherwise, both forms of the virus appeared similar in their mode of uptake. Entry occurs by fusion of the plasma membrane of the cell with the envelope surrounding the virus nucleocapsid at neutral pH. The receptor turnover for the virus probably occurs rapidly since saturation of receptor sites for the virus was not achieved. The binding and penetration of the virus, and the uncoating and transport of the viral genome to the nucleus is rapid. Uncoating occurs predominantly in the cytoplasm. The lower infectivity of PDV, compared with CRV, for cells in culture may happen because this form of the virus accumulates in cell vacuoles and is unable to proceed with infection.

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Baculovirus Replication: Phosphorylation of Polypeptides Synthesized in Trichoplusia ni Nuclear Polyhedrosis Virus-infected Cells

Cited by 24 publications

References 10 publications

Dynamic phosphorylation of Autographa californica nuclear polyhedrosis virus pp31

Dynamic phosphorylation of Autographa californica nuclear polyhedrosis virus pp31

Comparative Proteomics Reveal Fundamental Structural and Functional Differences between the Two Progeny Phenotypes of a Baculovirus

Baculovirus Replication: Uptake of Trichoplusia ni Nuclear Polyhedrosis Virus Particles by Insect Cells

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