Inhibition of productive replication of Epstein-Barr virus DNA by phosphonoacetic acid

Yuki, Yasuo; Tanaka, Akiko; Nonoyama, Meihan

doi:10.1016/0042-6822(76)90119-7

Cited by 71 publications

(31 citation statements)

References 5 publications

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“…It has been reported that superinfection of Raji cells with EBV obtained from P3HR1 cell cultures induced the production of EBV particles (SI Raji virus) but the virus thus produced did not superinfect Raji cells (5). In this study, however, we found DNA synthesis, similar to Raji cells superinfected with HR1 virus was observed (Fig.…”

Section: Establishment Of Human Lymphoblastoid Cellscontrasting

confidence: 54%

Transforming activity of Epstein-Barr virus obtained by superinfection of Raji cells.

Yuki¹,

Marczynska²,

Nonoyama³

1978

Proc. Natl. Acad. Sci. U.S.A.

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established by infection of human cord blood lymphocytes with SI Raji virus, were maintained in RPMI 1640 medium supplemented with 8% fetal calf serum. The medium contained 100 units of penicillin and 50 Mg of streptomycin per ml.Superinfection of Raji and HLB Cells. Raji cells and HLB cells were superinfected with HR1 virus in minimal essential medium lacking phosphate with 2% fetal calf serum as reported previously (5).Test for Transforming Activity of SI Raji Virus. Human cord blood was collected into syringes rinsed with preservative-free heparin and dextran was added to a final concentration of 1%. After the blood stood at 370 for 1 hr, cell-rich plasma was collected and the mononuclear leukocytes were separated from plasma on Ficoll-Hypaque gradients (6). Isolated leukocyte populations were incubated overnight in a humidified CO2 incubator at the concentration of 1 X 106 cells per ml in RPMI 1640 medium supplemented with 20% fetal calf serum. Leukocytes were collected by centrifugation at 1000 rpm for 10 min and resuspended in supernatant fluid of superinfected Raji cells (48 hr after superinfection) that had been made cell free by filtration through a nitrocellulose membrane filter (0.45 um pore size). After 1 hr of adsorption with occasional shaking, infected cells were washed once and then maintained at 106 cells per ml at 370 in RPMI 1640 medium containing 20% fetal calf serum. Half the medium was replaced with fresh medium weekly.Calculation of EBV Genome Content. EBV-specific cRNA was prepared in vitro from EBV DNA by using Escherchia coli RNA polymerase. Alkaline-denatured DNA in 0.90 M NaCl/ 0.090 M sodium citrate was passed through nitrocellulose membrane filters and single-stranded DNA was fixed to it by baking at 80°under reduced pressure for 2 hr. cRNA (1.

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Section: Establishment Of Human Lymphoblastoid Cellscontrasting

confidence: 54%

Transforming activity of Epstein-Barr virus obtained by superinfection of Raji cells.

Yuki¹,

Marczynska²,

Nonoyama³

1978

Proc. Natl. Acad. Sci. U.S.A.

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“…PAA inhibits the replication of EBV DNA (Yajima et al, 1976) but not that of host cells whereas HU prevents the replication of cellular DNA (Mele et al, 1974;Honess & Watson, 1977b); it is believed that HU does not inhibit the replication of DNA of superinfecting EBV (Wolf & Bayliss, 1979;Lamon & Lidin, 1979). Ara-C is known to be a rather effective inhibitor of total DNA synthesis.…”

Section: Dependence Of Virus-induced Protein Synthesis On Dna Replicamentioning

confidence: 99%

Herpesvirus Saimiri-induced Proteins in Lytically Infected Cells. I. Time-ordered Synthesis

Modrow¹,

Wolf²

1983

Journal of General Virology

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SUMMARYThe addition of TPA (phorbol-12-myristate-13-acetate) to cultures during the lytic infection with herpesvirus saimiri led to an enhanced and accelerated production of polypeptides induced by H. saimiri and to a rapid shut-down of host cell protein synthesis and allowed a detailed analysis of the protein patterns. Analysis of sequential protein synthesis in owl monkey kidney cells lytically infected with H. saimiri 11 permitted the identification of 31 virus-induced polypeptides. The use of the amino acid analogues canavanine (for arginine) and azetidine (for proline) in parallel allowed experiments on the identification of proteins synthesized early and late during lytic infection.

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“…Phosphonoacetic acid (PAA) has been previously shown to suppress replication of herpes simplex virus (1,19), avian herpesvirus (11), cytomegalovirus (9), Epstein-Barr virus (16,23,27), vaccinia virus, equine abortion virus, and varicella-zoster virus (1,18) in tissue culture. Promising results in the treatment of ocular, cutaneous, and encephalitic herpesvirus infections in mice, hamsters, and rabbits have been documented (4,5,14,17,21,25).…”

mentioning

confidence: 99%

Structure-activity studies on phosphonoacetate

Mao¹,

Otis²,

Esch³

et al. 1985

Antimicrob Agents Chemother

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Phosphonoacetic acid is a selective antiherpesvirus agent. More than 100 congeners of phosphonoacetic acid were evaluated in vitro and in vivo to understand structure-activity relationships in the hope of designing a superior analog. Results showed that the antiherpesvirus activity had highly specific structural requirements. Neither the carboxylic nor the phosphono groups could be replaced. The distance between these two groups is important. Increase of this distance caused complete loss of activity. However, if this distance was maintained, the addition of groups to the methylene carbon resulted in a reduction, but not loss, of activity. On the other hand, decrease of the carbon chain to formic acid did not deteriorate its antiherpes activity. All analogs tested had lower activity than the parent compound. However, some compounds with decreased activity in vitro appeared to have favorable pharmacological properties in vivo.

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Inhibition of productive replication of Epstein-Barr virus DNA by phosphonoacetic acid

Cited by 71 publications

References 5 publications

Transforming activity of Epstein-Barr virus obtained by superinfection of Raji cells.

Transforming activity of Epstein-Barr virus obtained by superinfection of Raji cells.

Herpesvirus Saimiri-induced Proteins in Lytically Infected Cells. I. Time-ordered Synthesis

Structure-activity studies on phosphonoacetate

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