The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication

Quinlan, Margaret P.; Chen, Lan Bo; Knipe, David M.

doi:10.1016/0092-8674(84)90035-7

Cited by 289 publications

(323 citation statements)

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“…HSV-1 replication centers develop in the nuclei of infected cells in a time-dependent manner. 42 Viral and cellular proteins required for viral DNA replication (such as the HSV-1 core replication proteins which include ICP8, the singlestranded DNA binding protein) and replicating viral DNA localize to these centers. [42][43][44][45] Mature HSV-1 replication centers were observed in the nuclei of V27 cells a b…”

Section: Replication Center Formation By D271-rcmentioning

confidence: 99%

High-titer recombinant adeno-associated virus production utilizing a recombinant herpes simplex virus type I vector expressing AAV-2 Rep and Cap

et al. 1999

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Recombinant adeno-associated virus type 2 (rAAV) vecderived cell line. Effective amplification of rAAV vectors tors have recently been used to achieve long-term, high introduced into 293 cells by infection was also demonlevel transduction in vivo. Further development of rAAV strated. Passage of rAAV with d27.1-rc results in up to 200-vectors for clinical use requires significant technological fold amplification of AAV-GFP with each passage after improvements in large-scale vector production. In order to coinfection of the vectors. Efficient, large-scale production facilitate the production of rAAV vectors, a recombinant (Ͼ10 9 cells) of AAV-GFP from a proviral cell line was also herpes simplex virus type I vector (rHSV-1) which does not achieved and these stocks were free of replication-comproduce ICP27, has been engineered to express the AAVpetent AAV. The described rHSV-1 vector provides a 2 rep and cap genes. The optimal dose of this vector, novel, simple and flexible way to introduce the AAV-2 rep d27.1-rc, for AAV production has been determined and and cap genes and helper virus functions required to proresults in a yield of 380 expression units (EU) of AAV-GFP duce high-titer rAAV preparations from any rAAV proviral produced from 293 cells following transfection with AAVconstruct. The efficiency and potential for scalable delivery GFP plasmid DNA. In addition, d27.1-rc was also efficient of d27.1-rc to producer cell cultures should facilitate the at producing rAAV from cell lines that have an integrated production of sufficient quantities of rAAV vectors for clini-AAV-GFP provirus. Up to 480 EU/cell of AAV-GFP could cal application. be produced from the cell line GFP-92, a proviral, 293

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Section: Replication Center Formation By D271-rcmentioning

confidence: 99%

High-titer recombinant adeno-associated virus production utilizing a recombinant herpes simplex virus type I vector expressing AAV-2 Rep and Cap

et al. 1999

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“…1) is introduced into cells by transfection (24,27 3). Therefore, these polypeptides were not related to ICP8 and did not contribute to the immunofluorescence observed specifically in cells transfected with pSG18 (24).…”

Section: Methodsmentioning

confidence: 99%

“…The amount of DNA in each mix (0.5 ml) was adjusted to 10 ,ug Immunoprecipitation. The procedures for preparation of cell extracts and immunoprecipitation with 39S monoclonal antibody were described previously (24). Proteins from the immunoprecipitates were analyzed in sodium dodecyl sulfate-polyacrylamide gels (18) that were treated for fluorography (19 The total DNA from transfected cells (10-,ug portions) was digested with ClaI, which cleaves once in the vector sequences of plasmid pSG18.…”

Section: Methodsmentioning

confidence: 99%

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Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions.

Quinlan¹,

Knipe²

1985

Mol. Cell. Biol.

244

235

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We examined the expression and localization of herpesvirus proteins in monkey cells transfected with recombinant plasmids containing herpes simplex virus (HSV) DNA sequences. Low levels of expression of the major HSV DNA-binding protein ICP8 were observed when ICP8-encoding plasmids were introduced into cells alone. ICP8 expression was greatly increased when a recombinant plasmid encoding the HSV alpha (immediate-early) ICP4 and ICPO genes was transfected with the ICP8 gene. Deletion and subcloning analysis indicated that two separate functions capable of stimulating ICP8 expression were encoded on the alpha gene plasmid. One mapped in or near the ICP4 gene, and one mapped in or near the ICPO gene. Their stimulatory effects were synergistic when introduced on two separate plasmids. Thus, two separate viral functions can activate herpesvirus early gene expression in transfected cells.Gene products encoded by animal viruses have provided some of the few examples of well-characterized eucaryotic functions that stimulate the expression of other viral and cellular genes. These provide excellent systems in which to study the mechanisms by which eucaryotic gene expression can be regulated. The adenovirus ElA function (3,14), the herpes simplex virus (HSV) ICP4 (5,16,23,32), and the pseudorabies virus immediate-early gene product (2) have been shown to activate expression of their respective early and late genes during the viral lytic cycles. The pseudorabies virus immediate-early gene product can complement the defective function of an ElA mutant virus (6). Therefore, it was hypothesized that these two functions operate through a common mechanism (6). The action of the simian virus 40 (SV40) large T antigen is somewhat more complicated in that it stimulates the expression of late SV40 genes while repressing early transcription (4, 15).The ElA or pseudorabies functions can stimulate the expression of viral and even cellular genes when these genes are introduced into cells with the marker gene by transfection (9, 13). It has been suggested that these functions stimulate transcription nonspecifically by inactivating an inhibitory cellular function (22) or promoting assembly of stable transcription complexes (7). Although genes introduced into cells by transfection are activated by ElA, similar genes in the cellular genome are not activated (9). Therefore, several levels of transcriptional regulation exist.Adenovirus VAl RNA has been shown to stimulate the translation of late adenoviral mRNAs during viral infection (31). Transfection of this gene into cells with an adenoviral gene also leads to an increase in translation of the mRNA (30). Therefore, viral gene products can affect the transcription of viral genes or the translation of viral mRNA. Many of these effects can be observed in cells transfected with the cloned viral regulatory genes.The HSV ICP8 DNA-binding protein is a beta (delayedearly) gene product whose expression depends on the synthesis of alpha (immediate-early) HSV proteins (12. 25 Plasmids. Escherichia c...

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“…The expression kinetics of the MCMV MDBP gene is consistent with the functi on of the MDB protein. In HSV-1 it was shown that the ICP8 protein migrates to prereplicative sites prior to DNA replication (Gao and Knipe, 1989), and it was proposed that ICP8 serves as organizational protein for targeting other replication proteins to these sites (Quinlan et al, 1984). For the HCMV and SCMV MDB proteins a subnuclear localization was observed which is reminiscent of the HSV-1 ICP8 protein (Anders et al, 1987;Kemble et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the murine cytomegalovirus genes encoding the major DNA binding protein and the ICP18.5 homolog

Messerle

Keil²,

Schneider

et al. 1992

Virology

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In several herpesviruses the genes for the major DNA binding protein (MDBP), a putative assembly protein, the glycoprotein B (gB), and the viral DNA polymerase (pol) coliocate. In murine cytomegalovirus (MCMV), two members of this gene block, pol (Elliott, Clark, Jaquish, and Spector, 1991, Virology 185, 169-186) and gB (Rapp, Messerle, BOhler, Tannheimer, Keil, and Koszinowski, 1992, J. Virol., 66,4399-4406) have been characterized. Here the two other MCMV genes are characterized, the gene encoding the MDBP and the ICP18.5 homolog encoding a putative assembly protein. Like in human cytomegalovirus (HCMV) the genes order is pol, gB, ICP18.5, and MDBP. The 4.2-kb MDBP mRNA is expressed first in the early phase, whereas the 3.0-kb ICP18.5 mRNA is a late transcript. The open reading frame of the MDBP gene has the capacity of encoding a protein of 1191 amino acids with a predicted molecular mass of 131.7 kDa. The MCMV ICP18.5 ORF is translated into a polypeptide of 798 amino acids with a calculated molecular mass of 89.1 kDa. Comparison of the amino acid sequences of the predicted proteins of MCMV with the respective proteins of HCMV, Epstein-Barr virus (EBV), and herpes simplex virus type-1 (HSV-1) reveals a striking homology ranging from 72% (HCMV), 50% (EBV), to 45% (HSV-1) for the MDBP sequence and from 74% (HCMV), 51 % (EBV), to 49% (HSV-1) for the ICP18.5 sequence. These results establish the elose relationship of the two cytomegaloviruses, and underline the usefulness of the murine model for studies on the biology of the CMV infection.

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The intranuclear location of a herpes simplex virus DNA-binding protein is determined by the status of viral DNA replication

Cited by 289 publications

References 51 publications

High-titer recombinant adeno-associated virus production utilizing a recombinant herpes simplex virus type I vector expressing AAV-2 Rep and Cap

High-titer recombinant adeno-associated virus production utilizing a recombinant herpes simplex virus type I vector expressing AAV-2 Rep and Cap

Stimulation of expression of a herpes simplex virus DNA-binding protein by two viral functions.

Characterization of the murine cytomegalovirus genes encoding the major DNA binding protein and the ICP18.5 homolog

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