Changes in the nucleoprotein complexes of a baculovirus DNA during infection

Wilson, Marijo E.; Miller, Lois K.

doi:10.1016/0042-6822(86)90052-8

Cited by 57 publications

(34 citation statements)

References 37 publications

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“…As infection progresses, production of cellular proteins is considerably reduced, while viral proteins begin to appear in increasing amounts. These changes culminate with the shutoff of cellular proteins synthesis (Carstens et al, 1979;Dobos and Cochan, 1980;Kelly and Lescott, 1981;Maruniak and Summers, 1981;Pennock et al, 1984;Rohel and Faulkner, 1984;Wilson and Miller, 1986). During AgMNPV infection of UFL-AG-286 cells, we noted a similar decrease in the number of proteins being synthesized at different times p.i.…”

Section: Changes In Protein Synthesis During Infectionmentioning

confidence: 55%

Structural and Ultrastructural Changes during the Infection of UFL-AG-286 Cells with the Baculovirus AgMNPV

Pombo¹,

Velloso²,

Ribeiro³

et al. 1998

Journal of Invertebrate Pathology

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Structural and Ultrastructural Changes during the Infection of UFL-AG-286 Cells with the Baculovirus AgMNPVVivian Pombo Lucas Malard Velloso Bergmann M. Ribeiro Sonia N. Báo AbstractDuring infection of the permissive insect cell line UFL-AG-286 by the baculovirus Anticarsia gemmatalis nucleopolyhedrovirus (AgMNPV-2D) several morphological changes occur. By 12 h postinfection (h p.i.), the infected cells became round and exhibited a decrease in the number of cytoplasmic projections. By 24 h p.i., it was possible to detect a virogenic stroma inside the cell nucleus, and after 48 h p.i., polyhedral inclusion bodies were observed. Some of these morphological modifications are probably due to changes in the cytoskeleton of the cell and this possibility was substantiated by the observation that the distribution of actin and microtubules was dramatically modified upon infection. Several viral-induced proteins were also produced during infection and a sharp decrease in overall protein synthesis was observed. These results are very similar to those obtained with other cell lines infected with different baculoviruses, indicating a similar mechanism of infection.

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Section: Changes In Protein Synthesis During Infectionmentioning

confidence: 55%

Structural and Ultrastructural Changes during the Infection of UFL-AG-286 Cells with the Baculovirus AgMNPV

Pombo¹,

Velloso²,

Ribeiro³

et al. 1998

Journal of Invertebrate Pathology

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“…Nucleocapsid maturation appears to begin with the assembly of empty capsid sheaths on the base structure. The nucleoprotein core, which is composed of a circular, covalently closed doublestranded DNA genome and the major basic protamine-like core protein P6.9 (46), is concentrated from the base to the apex of the capsid cylinder. The apical cap of the nucleocapsid is oriented toward the matte (13).…”

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confidence: 99%

Autographa californica Multiple Nucleopolyhedrovirus 38K Is a Novel Nucleocapsid Protein That Interacts with VP1054, VP39, VP80, and Itself

Liang

Kan

et al. 2008

J Virol

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It has been shown that the Autographa californica multiple nucleopolyhedrovirus (AcMNPV) 38K (ac98) is required for nucleocapsid assembly. However, the exact role of 38K in nucleocapsid assembly remains unknown. In the present study, we investigated the relationship between 38K and the nucleocapsid. Western blotting using polyclonal antibodies raised against 38K revealed that 38K was expressed in the late phase of infection in AcMNPV-infected Spodoptera frugiperda cells and copurified with budded virus (BV) and occlusionderived virus (ODV). Biochemical fractionation of BV and ODV into the nucleocapsid and envelope components followed by Western blotting showed that 38K was associated with the nucleocapsids. Immunoelectron microscopic analysis revealed that 38K was specifically localized to the nucleocapsids in infected cells and appeared to be distributed over the cylindrical capsid sheath of nucleocapsid. Yeast two-hybrid assays were performed to examine potential interactions between 38K and nine known nucleocapsid shell-associated proteins (PP78/83, PCNA, VP1054, FP25, VLF-1, VP39, BV/ODV-C42, VP80, and P24), three non-nucleocapsid shell-associated proteins (P6.9, PP31, and BV/ODV-E26), and itself. The results revealed that 38K interacted with the nucleocapsid proteins VP1054, VP39, VP80, and 38K itself. These interactions were confirmed by coimmunoprecipitation assays in vivo. These data demonstrate that 38K is a novel nucleocapsid protein and provide a rationale for why 38K is essential for nucleocapsid assembly.

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“…During nucleocapsid assembly, viral DNA is condensed and packaged with P6.9 to form a DNA-protein core within the capsid (41,56). At least a small part of P6.9 is present in the VS of infected Sf9 cells (42).…”

Section: Discussionmentioning

confidence: 99%

Autographa californica Multiple Nucleopolyhedrovirus orf132 Encodes a Nucleocapsid-Associated Protein Required for Budded-Virus and Multiply Enveloped Occlusion-Derived Virus Production

Yang

Wang

Yue

et al. 2014

J Virol

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Autographa californica multiple nucleopolyhedrovirus orf132 (named ac132) has homologs in all genome-sequenced group I nucleopolyhedroviruses. Its role in the viral replication cycle is unknown. In this study, ac132 was shown to express a protein of around 28 kDa, which was determined to be associated with the nucleocapsids of both occlusion-derived virus and budded virus. Confocal microscopy showed that AC132 protein appeared in central region of the nucleus as early as 12 h postinfection with the virus. It formed a ring zone at the periphery of the nucleus by 24 h postinfection. To investigate its role in virus replication, ac132 was deleted from the viral genome by using a bacmid system. In the Sf9 cell culture transfected by the ac132 knockout bacmid, infection was restricted to single cells, and the titer of infectious budded virus was reduced to an undetectable level. However, viral DNA replication and the expression of late genes vp39 and odv-e25 and a reporter gene under the control of the very late gene p10 promoter were unaffected. Electron microscopy showed that nucleocapsids, virions, and occlusion bodies were synthesized in the cells transfected by an ac132 knockout bacmid, but the formation of the virogenic stroma and occlusion bodies was delayed, the numbers of enveloped nucleocapsids were reduced, and the occlusion bodies contained mainly singly enveloped nucleocapsids. AC132 was found to interact with envelope protein ODV-E18 and the viral DNA-binding protein P6.9. The data from this study suggest that ac132 possibly plays an important role in the assembly and envelopment of nucleocapsids. IMPORTANCETo our knowledge, this is the first report on a functional analysis of ac132. The data presented here demonstrate that ac132 is required for production of the budded virus and multiply enveloped occlusion-derived virus of Autographa californica multiple nucleopolyhedrovirus. This article reveals unique phenotypic changes induced by ac132 deletion on the virus and multiple new findings on ac132.

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Changes in the nucleoprotein complexes of a baculovirus DNA during infection

Cited by 57 publications

References 37 publications

Structural and Ultrastructural Changes during the Infection of UFL-AG-286 Cells with the Baculovirus AgMNPV

Structural and Ultrastructural Changes during the Infection of UFL-AG-286 Cells with the Baculovirus AgMNPV

Autographa californica Multiple Nucleopolyhedrovirus 38K Is a Novel Nucleocapsid Protein That Interacts with VP1054, VP39, VP80, and Itself

Autographa californica Multiple Nucleopolyhedrovirus orf132 Encodes a Nucleocapsid-Associated Protein Required for Budded-Virus and Multiply Enveloped Occlusion-Derived Virus Production

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