Synthesis of Human Cytomegalovirus-specified RNA and Protein in Interferon-treated Cells at Early Times After Infection

Stinski, Mark F.; Thomsen, Darrell R.; Rodríguez, José

doi:10.1099/0022-1317-60-2-261

Cited by 26 publications

(26 citation statements)

References 41 publications

(26 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Analysis by polyacrylamide gel electrophoresis of the proteins synthesized at different times after infection indicated that there was no major difference between control and IFN-treated cells. We conclude from these results that the effect of IFN treatment on HSV-1 development is quite different from that previously reported for SV40 (Yakobson et al, 1977), vaccinia virus (Metz et al, 1975) and cytomegalovirus (Stinski et al, 1982), since herpesvirus protein synthesis evidently takes place in cells treated with HuIFNc¢(Ly).…”

Section: Effect Of Ifn Treatment On Virus Production Macromolecular contrasting

confidence: 82%

“…Although herpesviruses are sensitive to IFN and a number of reports indicate than IFN is a potent antiviral substance against herpesvirus infection in man (Dunnick & Galasso, 1979;Merigan, 1981), the molecular mechanism of action of human IFN against herpesvirus infection is unknown. According to a recent report, treatment of cells with human IFN before cytomegalovirus infection led to the inhibition of immediate-early protein synthesis and, perhaps as a consequence, to the suppression of early viral RNA synthesis (Stinski et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Formation of Non-infective Herpesvirus Particles in Cultured Cells Treated with Human Interferon

Múñoz

Carrasco

1984

Journal of General Virology

View full text Add to dashboard Cite

SUMMARY Treatment of HeLa cells with human lymphoblastoid interferon [HulFN-~(Ly)]induced an antiviral state that rendered the cells refractory to infection by herpes simplex virus type 1 (HSV-1), and the yield of infectious HSV-1 was reduced by 98%. Analysis of the mechanism of the anti-herpes action of IFN indicated that no gross inhibition of viral protein synthesis took place and late proteins appeared, although the synthesis of some of them was partially inhibited. No differences were apparent between the glycoproteins or phosphoproteins synthesized in control and IFN-treated HSV-l-infected HeLa cells. No inhibition of the formation of new virus particles from IFN-treated cells was evident as assessed by electron microscopy and biochemical analyses, although their infectivity was drastically reduced. These virions exhibited some differences in their content of a few proteins as determined by PAGE. Studies on the second infection cycle with virions obtained from IFN-treated cells suggested that they attached and penetrated HeLa cells but that their development was impaired, since no viral protein synthesis was observed during the second infection. Altogether these results do not support the idea that the molecular mechanism of action of human IFN against HSV-1 is mediated via the 2'-5'A system, or by the inactivation of initiation factors. Rather, they focus the problem of the anti-herpes action of IFN at the level of formation of defective virions.

show abstract

Section: Effect Of Ifn Treatment On Virus Production Macromolecular contrasting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

Formation of Non-infective Herpesvirus Particles in Cultured Cells Treated with Human Interferon

Múñoz

Carrasco

1984

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…HCMV infection poses very little threat to immunocompetent individuals but causes life-threatening complications in individuals with suppressed immune systems, such as patients with AIDS, patients with cancer undergoing chemotherapy, and organ transplant recipients treated with immunosuppressants (3)(4)(5). An intact IFN response is indispensable for limiting and clearing in vivo infections by the mouse homologue of HCMV (MCMV), and in vitro incubation of cells with IFN before MCMV or HCMV infection inhibits virus production (6)(7)(8)(9). However, the mechanism of IFN protection against CMV at the molecular level is not known.…”

mentioning

confidence: 99%

Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus

Chin

Cresswell

2001

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

366

399

View full text Add to dashboard Cite

Little is known about the mechanism by which IFNs inhibit human cytomegalovirus (HCMV) replication. Indeed, infection of fibroblasts with HCMV initiates the expression of a subset of type I IFN-inducible genes whose role in the infectious process is unclear. We describe here the identification of a cytoplasmic antiviral protein that is induced by IFNs, by HCMV infection, and by the HCMV envelope protein, glycoprotein B (gB). Stable expression of the protein in fibroblasts inhibits productive HCMV infection, down-regulating several HCMV structural proteins (gB, pp28, and pp65) known to be indispensable for viral assembly and maturation. We have named the protein viperin (for v irus i nhibitory p rotein, e ndoplasmic r eticulum-associated, in terferon-inducible). HCMV infection causes the redistribution of the induced viperin from its normal endoplasmic reticulum association, first to the Golgi apparatus and then to cytoplasmic vacuoles containing gB and pp28. Expression before HCMV infection reduces viperin redistribution from the endoplasmic reticulum to the Golgi apparatus and prevents vacuolar localization, perhaps reflecting the mechanism used by HCMV to evade the antiviral function.

show abstract

“…For example, immediate early gene expression of both HCMV and HSV is restricted but not abolished by IFN-␣/␤ (34,44,48,55). To minimalize antiviral responses activated during entry, herpesviruses have evolved various mechanisms to counter the cellular response.…”

mentioning

confidence: 99%

Kaposi's Sarcoma-Associated Herpesvirus Virions Inhibit Interferon Responses Induced by Envelope Glycoprotein gpK8.1

Perry

Compton

2006

J Virol

View full text Add to dashboard Cite

The Kaposi's sarcoma-associated herpesvirus (KSHV) envelope glycoprotein gpK8.1 contributes to cellular attachment through binding cell surface heparan sulfate proteoglycans. By using a soluble recombinant form of gpK8.1, we discovered that a consequence of gpK8.1 interaction with human fibroblasts is the induction of an antiviral response, as characterized by the activation of interferon regulatory factor 3 (IRF-3), production of interferon beta (IFN-␤), and expression of interferon-stimulated antiviral genes. In contrast, neither IFN-␤ expression nor a functional antiviral response is observed in cells treated with KSHV virions. The interferon response induced by soluble gpK8.1 can be inhibited by simultaneous treatment with UV-inactivated virions, while the induction of an indicator inflammatory cytokine, interleukin-6, was readily evident in the response to both gpK8.1 and KSHV. In addition, KSHV virions abrogate gpK8.1-mediated activation of IRF-3, an early transcriptional regulator for cellular antiviral responses. Although innate immune responses are initiated during contact between gpK8.1 and cellular receptor(s), these results suggest that the virion contains one or more structural elements that selectively repress an effective antiviral response while allowing cellular responses favorable to the KSHV life cycle.

show abstract

Synthesis of Human Cytomegalovirus-specified RNA and Protein in Interferon-treated Cells at Early Times After Infection

Cited by 26 publications

References 41 publications

Formation of Non-infective Herpesvirus Particles in Cultured Cells Treated with Human Interferon

Formation of Non-infective Herpesvirus Particles in Cultured Cells Treated with Human Interferon

Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus

Kaposi's Sarcoma-Associated Herpesvirus Virions Inhibit Interferon Responses Induced by Envelope Glycoprotein gpK8.1

Contact Info

Product

Resources

About