Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0268318 (ICP)
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The Epstein-Barr virus-carrying lymphoblastoid cell line Raji has two major genomic deletions and is incapable of virus production. Two cDNA clones, c70 and c55, were constructed from early mRNA of P3HR-1 cells and localized, respectively, in BALF-2 and BARF-1 open reading frames where one of the major genomic deletion in Raji cells is situated. These were used to search the different early viral transcripts in producer P3HR-1 and nonproducer Raji lines. c70 and c55 hybridized with their corresponding mRNAs only in producer lines. Analysis with in vitro-synthesized RNA probes showed quite a different transcriptional profile in Raji cells than in P3HR-1 cells. In the P3HR-1 line, BALF-2 encodes a 3.4-kilobase (kb) mRNA during the early phase and a 3.3-kb mRNA during the late phase, and in the Raji line, the probe corresponding to BALF-2 hybridized with three mRNAs of 5.0, 3.1, and 2.4 kb; in P3HR-1 cells, BARF-1 encodes a group of 3'-conterminal transcripts (0.8, 1.2, 1.7, 2.7, 3.2, and 5.0 kb) during both the early and late stages; in Raji cells, however, 0.8-, 1.2-, and 1.7-kb mRNAs are absent, the only mRNAs transcribed being upstream of the deletion and of 5.0, 2.6, and 2.0 kb in size. In vivo and in vitro experiments demonstrated that the BALF-2 open reading frame encodes an early 135-kilodalton (kDa) protein which possesses DNA-binding ability and can be recognized by a herpes simplex virus ICP-8 antiserum. The BARF-1 open reading frame encodes in vitro a 26- to 33-kDa early protein recognized by anti-EA serum. The proteins of both two genes expressed in psi AM 22b cells were localized in nuclei. According to their properties, both proteins, particularly the BALF-2-encoded 135-kDa DNA-binding protein, could play a role in virus replication.
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PMID:Altered expression of two Epstein-Barr virus early genes localized in BamHI-A in nonproducer Raji cells. 283 94

We have shown previously that the antiviral function of CD4+ T lymphocytes against murine cytomegalovirus (MCMV) is associated with the release of interferon-gamma (IFN-gamma). We now demonstrate that IFN-gamma and tumour necrosis factor alpha (TNF-alpha) display synergism in their antiviral activity. As little as 2 ng/ml of IFN-gamma and TNF-alpha reduced the virus yield by about three orders of magnitude. There was no effect on immediate early (IE) and early (E) gene expression as far as the candidate genes IE1, E1 and those encoding the major DNA-binding protein and the DNA polymerase were concerned. Late gene transcription, assayed by the candidate genes encoding glycoprotein B and the MCMV homologue of ICP 18.5, was blocked and MCMV DNA replication was found to be reduced but not halted. The most prominent finding of the cytokine effect, seen by electron microscopy, was an alteration of nucleocapsid formation. Altogether, the synergism is multifaceted and acts at more than one stage during viral morphogenesis. Because the cytokines clearly do not act at an early stage of infection we conclude that the mode of cytokine activity differs between alpha- and betaherpesviruses.
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PMID:Late phase inhibition of murine cytomegalovirus replication by synergistic action of interferon-gamma and tumour necrosis factor. 811 18

The nucleotide sequence of a region encompassing about 5,200 base pairs (bp) of the left side of the origin of replication in the long unique region of the herpes simplex virus type 2 (HSV-2) has been determined. This region contained the major DNA-binding protein or the infected-cell protein 8 (ICP 8) gene and 5'-part of the counterpart of HSV-1 ICP 18.5 gene. A comparison of the nucleotide sequence of the ICP8 gene between HSV-1 and HSV-2 showed an 89.8% homology. A primer extension analysis for the HSV-2 ICP 8 mRNA showed that the major transcriptional start site was mapped at 315 bp upstream of the initiation codon. A comparison of the predicted functional amino acid sequence of the ICP 8 between HSV-1 and HSV-2 revealed a striking homology (97.2%), the value of which was the highest among those of the other polypeptides encoded by HSV-1 and HSV-2. Some domains, which were shown to be required for the nuclear function, the binding to single-stranded DNA and the nuclear localization were well conserved. In addition, the nucleotide and the functional amino acid sequences of a part of the HSV-2 counterpart of the HSV-1 ICP 18.5 gene were also compared, demonstrating an 88.4% and 95.9% homology, respectively.
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PMID:Nucleotide sequence of the major DNA-binding protein gene of herpes simplex virus type 2 and a comparison with the type 1. 838 14