Immunogold Detection of Polyhedrin, p10 and Virion Antigens in Autographa californica Nuclear Polyhedrosis Virus-infected Spodoptera frugiperda Cells

Wilk, F. van der; Lent, J.W.M. van; Vlak, Just M.

doi:10.1099/0022-1317-68-10-2615

Cited by 74 publications

(46 citation statements)

References 18 publications

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“…5b) have been seen to accumulate in the cytoplasm and nucleus of cells infected with nuclear polyhedrosis viruses (Harrap, 1970;MacKinnon et al, 1974;Chung et al, 1980). The speculation that p 10 is a major component of these structures is supported by recent immunocytochemicat observations (van der Wilk et al, 1987) and the finding that the structures are absent in cells infected with the pl0 deletion mutants (Fig. 6, 7).…”

Section: Discussionsupporting

confidence: 63%

“…as a discrete structure. 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.…”

Section: Discussionmentioning

confidence: 99%

“…Recent investigations have indicated that pl0 shares antigenic similarities with some cytoskeletal elements (Quant-RusseU et al, 1987); in addition, the structures associated with pl0 in vitro have been identified as large fibrillar masses which accumulate in the host cytoplasm and nucleus (van der Wilk et al, 1987). The fibrillar masses failed to develop in cells infected with a neomycin phosphotransferase insertional pl0 mutant (Croizier et al, 1987), and a pl0/fl-galactosidase (fl-gal) fusion (deletion) mutant (Vlak et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

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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: Discussionsupporting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…4c). The association of pl0 with fibrillar structures has also been reported for the AcMNPV by van der Wilk et al (1987). The pl0 MAb also was associated with virions and polyhedra (Fig.…”

Section: Pio : Cross-reaction Of the Plo Mab With A Cellular Proteinmentioning

confidence: 49%

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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“…Similar structures were observed within the cell bodies of all control cells infected either with wild type virus or beta-galactosidase inserts . It looked very similar to the fibrous virally encoded p10 protein present in the cell bodies of the infected cells (Van Der Wilk et al ., 1987), with the exception that the material in the processes was kept within straight boundaries. It is therefore possible that the electrondense structure represents the p10 viral gene product .…”

Section: Ultrastructure Of Tau-induced Processesmentioning

confidence: 83%

Overexpression of tau in a nonneuronal cell induces long cellular processes.

Knops

Kosik

Lee

et al. 1991

The Journal of Cell Biology

268

113

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Abstract. The ways in which the various microtubuleassociated proteins (MAPS) contribute to cellular function are unknown beyond the ability of these proteins to modify microtubule dynamics. One member of the MAP family, tau protein, is restricted in its distribution to the axonal compartment of neurons, and has therefore prompted studies that attempt to relate tau function to the generation or maintenance of this structure. Sf9 cells from a moth ovary, when infected with a baculovirus containing a tau cDNA insert, elaborate very long processes . This single gene product expressed in a foreign host cell grossly alters the

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Immunogold Detection of Polyhedrin, p10 and Virion Antigens in Autographa californica Nuclear Polyhedrosis Virus-infected Spodoptera frugiperda Cells

Cited by 74 publications

References 18 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

Overexpression of tau in a nonneuronal cell induces long cellular processes.

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