Characterization of baculovirus p10 synthesis using monoclonal antibodies

Quant-Russell, R.L.; Pearson, Margot; Rohrmann, George F.; Beaudreau, G. S.

doi:10.1016/0042-6822(87)90038-9

Cited by 66 publications

(46 citation statements)

References 28 publications

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“…Van der Wilk et al (1987) speculated that the cytoplasmic accumulations may act as reservoirs of pl0. However, Quant-Russell et al (1987) demonstrated a crossreactivity of some pl0 monoclonal antibodies to the cytoskeleton. The distinct morphology of the cytoplasmic pl0 bodies, their persistence through infection, and the antigenic similarity to cytoskeletal elements are not consistent with the proposed functionless storage form of the molecule.…”

Section: Discussionmentioning

confidence: 99%

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

Williams

Rohel²,

Kuzio

et al. 1989

Journal of General Virology

143

100

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SUMMARYThe role of the Autographa cali]brniea nuclear polyhedrosis virus pl0 gene in viral cytopathology and morphogenesis was examined using classes of pl 0 deletion mutants with and without lacZ (fl-galactosidase) gene fusion. Mutant-infected cells did not form the fibrillar cytoplasmic and nuclear structures normally observed late in infection with wild-type (wt) virus, and the cells failed to lyse even at 2 weeks post-infection. Based on wt and mutant cytopathology, we suggest lysis may be facilitated by stepwise exhaustion of the host nuclear membrane, and may require a function resident in the carboxy region of p 10; this portion of the molecule is also essential for formation of the p 10-rich fibrillar bodies. Additional changes in cytopathology were correlated with the level of p 10/LacZ fusion protein expression. The insertional mutant designated Ac229, which encodes 51 N-terminal amino acids of pl0 fused to LacZ, caused intranuclear accumulation of granular structures at sites corresponding to the fibrillar bodies of wt viral infections. Occlusion body membranes, which associate with the fibrillar bodies in wt infections, were also formed in mutant virus-infected cells. However, membranes did not associate with occlusion bodies in Ac229 infections, and were aberrantly attached to occlusion bodies in cells infected with mutants having simple p 10 deletions (represented by Ac231). Loss of the outer membrane increased sensitivity of the occlusion bodies to disruption by physical stress; a partially attached membrane afforded some protection from disruption.

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Section: Discussionmentioning

confidence: 99%

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

Williams

Rohel²,

Kuzio

et al. 1989

Journal of General Virology

143

100

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“…The PE protein has also been observed to associate with the periphery of prominent infected cell-specific fibril-like structures (Russell & Rohrmann, 1990). In addition, a hyperexpressed protein, pl0, has been found associated with polyhedra (Quant- Russell et al, 1987) and also with the fibrillar structures (Vlak et al, 1988). P10 appears to play a role in the proper assembly of polyhedra, as it has been demonstrated that p 10-minus virus recombinants produce polyhedra which are unstable and readily fracture (Williams et al, 1989), with polyhedron envelopes that are incomplete or absent (Vlak et al, 1988;Williams et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

“…Polyhedrin is not observed on Western blots until 48 h p.i. (Bradford et al, 1990) (Quant -Russell et al, 1987). The PE protein is also a very late expressed protein and is not detected until 36 to 48 h p.i.…”

Section: Introductionmentioning

confidence: 99%

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Immunoelectron microscopic examination of Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus-infected Lymantria dispar cells: time course and localization of major polyhedron-associated proteins

Russell

Pearson²,

Rohrmann³

1991

Journal of General Virology

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Immnnoelectron microscopy was employed to examine the temporal expression and localization of two proteins involved in baculovirus polyhedron assembly (polyhedrin and p 10) of Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus (OpMNPV) in infected Lymantria dispar cells. In addition, the association of p 10 with the polyhedron envelope (PE) protein was studied. The major capsid protein (p39) was also examined to investigate the association of virion structural proteins with polyhedron formation. In infected cells, p39 did not show a concentrated association with any infected-cell structures other than nucleocapsids and appeared to be randomly distributed over the nucleocapsid surface. Likewise, polyhedrin showed no major concentrations outside of developing or mature polyhedra. The pl0 antibody cross-reacted with a protein associated with condensed chromosomes in uninfected cells. In infected cells, pl0 is a component of the body of fibrillar structures. The PE protein has been shown to accumulate around the periphery of fibrillar structures. Cells infected with a polyhedrin-minus virus expressing the fl-galactosidase gene under the control of the polyhedrin promoter were examined to determine whether the lack of polyhedra would influence the localization of major polyhedronassociated viral proteins. High concentrations of PE protein accumulating on the periphery of fibrillar structures appeared to be the major difference from wild-type virus-infected cells. The fl-galactosidase protein appeared to be distributed throughout the nucleus and cytoplasm, in contrast with the specific localization of the viral proteins.

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“…Regulation of the transition from budded to occluded virus is not well understood. It is known, however, that two viral proteins, polyhedrin and p10, are highly expressed late in infection and are involved in the occlusion of ODV (15)(16)(17). Though highly expressed in infected cells, polyhedrin and p10 are not required for BV production.…”

Section: Introductionmentioning

confidence: 99%

Copper Treatment Increases Recombinant Baculovirus Production and Polyhedrin and p10 Expression

et al. 1997

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Characterization of baculovirus p10 synthesis using monoclonal antibodies

Cited by 66 publications

References 28 publications

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

A Cytopathological Investigation of Autographa californica Nuclear Polyhedrosis Virus p10 Gene Function Using Insertion/Deletion Mutants

Immunoelectron microscopic examination of Orgyia pseudotsugata multicapsid nuclear polyhedrosis virus-infected Lymantria dispar cells: time course and localization of major polyhedron-associated proteins

Copper Treatment Increases Recombinant Baculovirus Production and Polyhedrin and p10 Expression

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