Intracellular location of rabbit poxvirus nucleic acid within infected cells as determined by in situ hybridization

Minnigan, Hal; Moyer, Richard W.

doi:10.1128/jvi.55.3.634-643.1985

Cited by 18 publications

(5 citation statements)

References 23 publications

(18 reference statements)

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“…The SP viral antigen in both cytoplasm and nucleus, sometimes only in the nuclei of some SPCs without evidence of cytoplasmic immunostaining, was found in the present study. However, the nuclear staining of some SPCs observed in the present study might be due to an artifact after tissue preparation, as reported by other workers ( Minnigan & Moyer 1985; Moss 1996).…”

Section: Discussionsupporting

confidence: 80%

“…On the other hand, the data from HeLa cell culture demonstrated that vaccinia virus‐induced DNA is synthesized within nuclei and is not as a result of cytoplasmic contamination ( LaColla & Weissbach 1975; Archard 1983). However, Minnigan & Moyer (1985) reported that rabbit pox virus DNA is located only within the cytoplasm, by in situ hybridization, and no evidence that viral DNA enters the cell nucleus, and that it must be considered as an artifact. In contrast, Mohanty et al .…”

Section: Discussionmentioning

confidence: 99%

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Immunohistochemical Detection of Antigen in Lamb Tissues Naturally Infected with Sheeppox Virus

Gülbahar¹,

Çabalar²,

Gül³

et al. 2000

Journal of Veterinary Medicine, Series B

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The present study describes the detection of sheeppox virus antigen in various lamb tissues, using an immunohistochemical technique, in sheeppox cases which occurred naturally. Sheeppox viral antigen was detected in the cytoplasm of sheeppox cells and degenerated epithelial cells of the skin, lungs and digestive tract involving typical sheeppox lesions. Nuclear staining was also observed in some typically deformed nuclei of sheeppox cells. The immunostaining of sheeppox virus showed a correlation with the presence of sheeppox cells and degenerated epithelial cells resembling them. Additionally, in order to confirm the presence of sheeppox virus in the skin and lung samples, direct electron microscopy was performed and sheeppox virus was only demonstrated in two skin samples.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Immunohistochemical Detection of Antigen in Lamb Tissues Naturally Infected with Sheeppox Virus

Gülbahar¹,

Çabalar²,

Gül³

et al. 2000

Journal of Veterinary Medicine, Series B

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“…The cytoplasmic site of vaccinia virus replication enabled us to express each protein in a cell whose nucleus was devoid of polyomavirus DNA. Although there have been some reports of the presence of vaccinia virus DNA associated with isolated nuclei from infected cells, in situ hybridization studies with the closely related rabbit poxvirus support an exclusively cytoplasmic localization (38).…”

Section: The Addition Of Phosphorylasementioning

confidence: 95%

Expression of polyomavirus virion proteins by a vaccinia virus vector: association of VP1 and VP2 with the nuclear framework

Stamatos¹,

Chakrabarti²,

Moss³

et al. 1987

J Virol

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The polyomavirus proteins VP1, VP2, and VP3 move from their cytoplasmic site of synthesis into the nucleus, where virus assembly occurs. To identify cellular or viral components which might control this process, we determined the distribution of VP1, VP2, and VP3 in a soluble fraction, a cytoplasmic cytoskeleton fraction, and a nuclear framework fraction of infected cells. All three proteins were detected in a detergent-extractable form immediately after their synthesis in polyomavirus-infected cells. Approximately 50, 25, and 40% of pulse-labeled VP1, VP2, and VP3, respectively, associated with the skeletal framework of the nucleus within 10 min after their synthesis. The remaining portion of each labeled protein failed to accumulate on the nuclear framework during a 40-min chase and was degraded. When expressed separately by recombinant vaccinia viruses, VP1 and VP2, but not VP3, accumulated on the nuclear framework. This association was not dependent on other polyomavirus proteins or viral DNA. The amount of total VP1 and VP2 which was bound to the nuclear framework approximated 45 and 20%, respectively. Indirect immunofluorescence demonstrated an exclusive nuclear localization of VP1 in situ. In coinfection experiments, a greater percentage of total VP2 and VP3 was bound to the nuclear framework of cells which cosynthesized VP1. These results indicate that although VP1 and VP2 can bind independently to the insoluble nuclear framework, the association of VP3 with this nuclear structure is promoted by the presence of VP1.

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“…Cytoplasmic NCLDV develop a transitory organelle, the virion factory, where all replication processes take place ( 12 – 15 ). The simultaneous delivery from the virion of the fully virally-encoded transcription apparatus together with the genomic DNA, allows the immediate transcription of the early expressed viral genes independently from the host machinery ( 13 , 16 – 20 ). As expected, all the Mimiviridae infecting Acanthamoeba (belonging to the mimiviruses sub-family) share the same transcriptional regulatory elements.…”

Section: Introductionmentioning

confidence: 99%

mRNA maturation in giant viruses: variation on a theme

Priet

Lartigue

Debart

et al. 2015

Nucleic Acids Research

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Giant viruses from the Mimiviridae family replicate entirely in their host cytoplasm where their genes are transcribed by a viral transcription apparatus. mRNA polyadenylation uniquely occurs at hairpin-forming palindromic sequences terminating viral transcripts. Here we show that a conserved gene cluster both encode the enzyme responsible for the hairpin cleavage and the viral polyA polymerases (vPAP). Unexpectedly, the vPAPs are homodimeric and uniquely self-processive. The vPAP backbone structures exhibit a symmetrical architecture with two subdomains sharing a nucleotidyltransferase topology, suggesting that vPAPs originate from an ancestral duplication. A Poxvirus processivity factor homologue encoded by Megavirus chilensis displays a conserved 5′-GpppA 2′O methyltransferase activity but is also able to internally methylate the mRNAs’ polyA tails. These findings elucidate how the arm wrestling between hosts and their viruses to access the translation machinery is taking place in Mimiviridae.

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Intracellular location of rabbit poxvirus nucleic acid within infected cells as determined by in situ hybridization

Cited by 18 publications

References 23 publications

Immunohistochemical Detection of Antigen in Lamb Tissues Naturally Infected with Sheeppox Virus

Immunohistochemical Detection of Antigen in Lamb Tissues Naturally Infected with Sheeppox Virus

Expression of polyomavirus virion proteins by a vaccinia virus vector: association of VP1 and VP2 with the nuclear framework

mRNA maturation in giant viruses: variation on a theme

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