Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Prostaglandins of the A series potently inhibited the production of vaccinia virus in mouse L fibroblasts. With the highest non-toxic dose of PGA1, 4 micrograms/ml, the replication of the virus was inhibited by 95 . 3%. The antiviral activity was dose-dependent and specific for the A series. At the dose used, PGA1 was not toxic to uninfected cells and did not alter cell metabolism as measured by DNA, RNA and protein synthesis. PGA1 did not influence the adsorption of the virus by the host cells and the antiviral activity was not dependent on the presence of PGA1 during the early stages of infection. PGA treatment delayed and partially inhibited virus DNA synthesis and, while it did not produce any change in the pattern of protein synthesis in uninfected cells, it altered both the rate and the pattern of virus protein synthesis. We conclude that PGA1 selectively inhibits one or more steps involved in the replication of vaccinia virus in mouse L fibroblasts.
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PMID:Antiviral effect of prostaglandins of the A series: inhibition of vaccinia virus replication in cultured cells. 618 27

The relationship between prostaglandins (PG) and interferon (IFN) was investigated. IFN induced the synthesis of immunoreactive PGE and PGA at early and late stages, respectively, of vaccinia virus infection in mouse L fibroblasts. Only species-specific IFN possessed this activity and PG synthesis was stimulated in virus-infected cells, while normal L cells were not affected. The vaccinia virus infection did not significantly alter PG synthesis in the absence of IFN. Indomethacin increased the rate of vaccinia virus replication and partially inhibited the IFN-induced protection of L cells. The addition of exogenous PGA1 only partially reversed this effect. Finally, short-term PGA treatment induced the synthesis of two enzymes (protein kinase and 2,5A synthetase) thought to be partially responsible for the antiviral action of interferon. These findings suggest that a prostaglandin or PG-related compound seems to mediate at least one aspect of IFN action.
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PMID:The relationship between the antiviral action of interferon and prostaglandins in virus-infected murine cells. 619 67

We have previously shown that prostaglandins of the A series are potent inhibitors of the replication of several animal viruses in cultured cells. In this report we have studied the mechanism of the antiviral action of PGA1 in vaccinia virus-infected mouse L cells, where there is an alteration in both the rate and extent of the synthesis of some virus proteins. When cytoplasmic RNAs from PGA-treated, vaccinia virus-infected cells were translated in cell-free systems, similar selective inhibition of the synthesis of some viral polypeptides was observed. The lack of translation of some viral RNAs was not due to an impairment of the methylation process nor to a difference in ionic requirements. PGA1, even at doses as high as 10 micrograms/ml, did not exert any direct inhibitory action on transcription in vitro as measured in two cell-free systems, and had no effect on primary transcription-translation of vaccinia virus RNAs when assayed in coupled cell-free systems. Southern blot hybridization analysis of cytoplasmic RNAs to EcoRI restriction fragments of vaccinia DNA showed that PGA1 was able to induce major changes in the pattern of RNA transcripts during the course of viral infection. We propose that changes in the transcription programme of vaccinia virus RNAs could be due either to an alteration of specific viral proteins that regulate transcription by direct binding of PGA1, or to the synthesis and/or activation of a host product that mediates the antiviral action.
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PMID:Selective inhibition of viral gene expression as the mechanism of the antiviral action of PGA1 in vaccinia virus-infected cells. 669 23

The effects of a number of crystalline and highly purified enzymes on elementary bodies of vaccinia are reported. These effects have been followed by determination of amino nitrogen, staining reaction, and studies of infectivity. Pepsin, at a pH which inactivates the virus, results in its solution and rapid release of amino nitrogen. Crystalline trypsin, chymotrypsin, carboxypeptidase, and ribonuclease are without appreciable effect on the virus. Papain within a short time produces profound alteration in the staining reaction of the elementary body with release of amino nitrogen accompanied by complete inactivation of the virus. This reaction is not shared by crystalline ficin, another plant papain, or by cathepsin, an intracellular proteinase analogous to plant papains but of animal origin.
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PMID:CONSTITUENTS OF ELEMENTARY BODIES OF VACCINIA : III. THE EFFECT OF PURIFIED ENZYMES ON ELEMENTARY BODIES OF VACCINIA. 1987 Oct 53