Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0268318 (ICP)
 10,007 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In cells infected with herpes simplex virus, HSV-I, newly synthesized polypeptides accumulated in the nucleus at different rates, which did not change during the first 6 h after infection. Canavanine, an arginine analogue, prevented the nuclear accumulation of ICP (infected cell polypeptides) 5 and 8 and azetidine, a proline analogue, prevented that of ICP 5 and 7. The transfer of polypeptides to the nucleus was inhibited at 4 degrees C but not by dinitrophenol. Some of the nuclear polypeptides could be released by washing isolated nuclei with hypertonic salt solutions. ICP 17 was particularly sensitive to high salt treatment while ICP 5 and II were resistent. ICP 4b, a modified form of the alpha polypeptide ICP 4, was released by EDTA, and the detergent NP40 removed ICP II. Treatment of nuclei with DNase selectively reduced the amount of bound alpha polypeptides ICP 4c (the second modified form of ICP 4), 0 and 27 as well as ICP 8 and 25. Nuclei isolated from infected or uninfected cells and incubated in labelled cytoplasmic extracts took up primarily ICP 8 and 32. Alpha polypeptides were taken up to a lesser extent and ICP 6 and 10 were excluded. It is concluded that affinities for various constituents of host cell nuclei are likely to determine the nuclear accumulation of specific virus polypeptides.
J Gen Virol 1978 Jun
PMID:On the association of virus proteins with the nuclei of cells infected with herpes simplex virus. 20 19

In cells infected with herpes simplex virus a protein associated with the small subunit of ribosomes became phosphorylated. It was not detectably labelled with 14C-amino acids added after infection and is therefore probably a cellular protein. The phosphorylated ribosomal proteins from HSV-1- and HSV-2-infected cells were indistinguishable electrophoretically and had an apparent mol. wt. of about 48 000. Phosphorylation of the 48K protein was detected 2 to 3 h after infection and reached a maximum rate at 4 to 5 h. It was prevented by adding cycloheximide at 2 h, or actinomycin at 1.5 h p.i., or azetidine at the beginning of infection. The phosphorylation did not occur on reversal of a cycloheximide block in the presence of actinomycin, confirming that it is not caused by a virus alpha-polypeptide. Virus that had been irradiated with u.v. light, although still able to suppress synthesis of cellular protein and DNA, did not induce phosphorylation of the 48K ribosomal protein. Therefore the phosphorylation is not responsible for the suppression of host synthesis. The alpha polypeptides ICP 4, 0, 22 and 27 are also phosphorylated but, in contrast to that of the ribosomal protein, their phosphorylation does not depend on the synthesis of beta and gamma polypeptides. It is probably mediated by a host enzyme.
J Gen Virol 1979 Nov
PMID:Phosphorylation of a ribosomal protein and of virus-specific proteins in cells infected with herpes simplex virus. 23 30

A 3698 bp region of the genome of infectious laryngotracheitis virus (ILTV) was sequenced and found to contain the entire glycoprotein gB gene and the C-terminal region of a gene homologous to the ICP 18.5 protein gene of herpes simplex virus type 1. The ILTV gB gene encoded a protein with an Mr of 100K possessing all the characteristics of a transmembrane glycoprotein. Alignment of the ILTV gB sequence with homologous sequences from six other herpesviruses revealed that 10 cysteine residues on the surface of the molecule were completely conserved and that the positions of several N-linked glycosylation sites were largely conserved. Evolutionary trees based on the gB amino acid sequences from a total of 13 herpesviruses were constructed and the relationships among these herpesviruses were examined.
J Gen Virol 1991 Feb
PMID:The nucleotide sequence of the glycoprotein gB gene of infectious laryngotracheitis virus: analysis and evolutionary relationship to the homologous gene from other herpesviruses. 184 76

A gene in equine herpesvirus 1 (EHV-1; equine abortion virus) equivalent to the gB glycoprotein gene of herpes simplex virus (HSV) has been identified by DNA hybridization and nucleotide sequencing. A 4.3 kbp EHV-1 PstI-ClaI sequence (0.40 to 0.43 map units) contained an open reading frame flanked by appropriate control elements and was capable of encoding a polypeptide of 980 amino acids. This had 50 to 60% identity over a 617 amino acid conserved region with the gB gene products of HSV and three other alphaherpesviruses, and 20 to 30% identity with those of human cytomegalovirus and Epstein-Barr virus. Analysis of the amino acid sequence predicts a long signal peptide, hydrophobic and hydrophilic domains and N-glycosylation sites, and has identified a probable internal proteolytic cleavage site. The EHV-1 gB open reading frame appears to be overlapped at its 5' end by 135 nucleotides of the 3' end of an upstream open reading frame the potential translation product of which has approximately 50% identity with HSV gene ICP 18.5 and VZV gene 30 products.
J Gen Virol 1989 Feb
PMID:Identification and nucleotide sequence of a gene in equine herpesvirus 1 analogous to the herpes simplex virus gene encoding the major envelope glycoprotein gB. 254 44

Five monoclonal antibodies to the alkaline nuclease of herpes simplex virus (HSV) types 1 and 2 have been used in immunoperoxidase tests to demonstrate the nuclear localization of the enzyme within HSV-1- and HSV-2-infected cells and to purify the enzyme from cells infected with either virus by immunoadsorbant chromatography. Affinity chromatography with a 32P-labelled extract of HSV-2-infected cells has enabled us to demonstrate that the nuclease eluting from the immunoadsorbant is a phosphoprotein, hence confirming the nuclease to be identical to the phosphorylated polypeptide previously referred to as ICSP 22 (HSV-2) or ICP 19 (HSV-1). In addition, the results clearly demonstrate that monoclonal antibodies Q1, CC1 and CH2 are directed against HSV type-common epitopes while V1 and T2T1 antibodies are against HSV-2-specific epitopes on the enzyme. Using the type-specific monoclonal antibodies in an immunoperoxidase test, the enzyme specified in cells infected with intertypic recombinants has been typed; correlation of these data with restriction endonuclease maps of the recombinants has enabled us to map the position of the active site of the nuclease gene to map units 0.168 to 0.184 on the genomes of both HSV-1 and HSV-2. Taken with the data mapping the mRNA encoding this enzyme, the nuclease active site can be mapped to 0.168 to 0.175 on the genome. Finally, the use of monoclonal antibodies in immunofluorescence tests on infected cells has demonstrated that the nuclease is synthesized within 2 h post-infection.
J Gen Virol 1985 Jan
PMID:Studies on the herpes simplex virus alkaline nuclease: detection of type-common and type-specific epitopes on the enzyme. 257 50

The localization of ICP 4, ICP 8, DNA polymerase and alkaline exonuclease within herpes simplex virus type 1 (HSV)-infected cells has been examined by immunofluorescence using specific antibodies to these proteins. Cells were simultaneously counterstained with the DNA-binding fluorochrome 4,6-diamidino-2-phenylindole (DAPI) to reveal the intranuclear distribution of DNA. These studies showed that in the absence of virus DNA replication ICP 4, ICP 8 and DNA polymerase were diffusely distributed throughout the nucleus but during virus DNA replication these proteins accumulated at specific foci within the nucleus. Initially these foci were near the nuclear membrane but with continuing virus DNA replication they increased in size until the whole of the nucleus became affected. The increase in size of these foci was coincident with a redistribution of nuclear DNA and margination of chromatin at the nuclear membrane, as revealed by DAPI staining. The number of foci initially present in an infected cell was dependent on the multiplicity of infection. The distribution of ICP 4, ICP 8 and DNA polymerase within the nucleus was altered by treating the cells with DNase. The majority of alkaline exonuclease was diffusely distributed throughout the nucleus during virus DNA replication and did not localize at specific foci within the nucleus. Autoradiographic examination of the incorporation of [3H]thymidine in cells infected with HSV showed that viral DNA replication occurred in restricted areas within the nucleus that were similar, in terms of number, location and size, to the foci where ICP 4, ICP 8 and DNA polymerase accumulated. Furthermore, in cells blocked in mitosis following infection with HSV, ICP 4, ICP 8 and DNA polymerase, but not alkaline exonuclease, localized in areas outside the condensed chromatin structures. DAPI staining revealed the presence of DNA in these areas and, as such structures were never seen when uninfected cells had entered mitosis, it is suggested that this extrachromosomal DNA is of viral origin. These studies therefore suggest that ICP 4 is associated with progeny virus DNA and that while its intranuclear localization is initially at non-viral sites, as DNA replication proceeds so ICP 4 is recruited into areas of virus DNA transcription and replication.
J Gen Virol 1986 Oct
PMID:Intranuclear localization of herpes simplex virus immediate-early and delayed-early proteins: evidence that ICP 4 is associated with progeny virus DNA. 302 Jan 58

The synthesis of alpha (immediate-early) polypeptides in Vero cells infected with pseudorabies virus was studied. Cycloheximide was added at the beginning of infection and removed several hours later. The accumulated alpha mRNA was translated either in vivo in the presence of actinomycin D to prevent further mRNA synthesis, or in vitro. In intact cells three electrophoretically distinct virus-specific proteins were synthesized, with apparent molecular weights of approximately 180 000 (A), 190 000 (B) and 200 000 (C). The accumulation of B and C was prevented by the proline analogue azetidine. Only protein A was detected in vitro. Proteins B and C were not detected in normally infected cells. All three were associated with the nuclear fraction of cell homogenates and A and B were phosphorylated. The radioactivity of B and C declined during a chase period while that of A increased. This change was prevented by adding cycloheximide during the chase. The pattern of chymotrypsin digestion products suggested that A and B at least were similar proteins. It is presumed that protein A is the single immediate-early protein previously described and analogous to ICP 4 of herpes simplex virus. The significance and function, if any, of proteins B and C is not known but it is possible that they represent stages in the formation or transport of A within the cell and that the progression depends on an unstable protein which is depleted in cells treated with cycloheximide.
J Gen Virol 1984 Sep
PMID:Synthesis of alpha (immediate-early) proteins in Vero cells infected with pseudorabies virus. 608 77

In Vero cells incubated at 40 degrees C or treated with azetidine at 37 degrees C, synthesis of a polypeptide ('C') of apparent mol. wt. 66000 was stimulated. It was not phosphorylated and was found in the cytoplasmic fraction of cell lysates. In cells infected with herpes simplex virus type 1 (HSV-1) in the presence of azetidine, synthesis of cellular proteins, including polypeptide C, was suppressed and infected cell polypeptides ICP 4, 0, 22 and 27 (apparent mol. wt. 170000, 120000, 75000 and 60000, respectively) were made. All were phosphorylated and accumulated in the nucleus. Messenger RNA for the same four polypeptides was made in cells infected in the presence of cycloheximide. Thus, ICP 22 is distinct from cellular polypeptide C and is probably a virus-specific alpha polypeptide, although it differs from alpha ICP 4, 0 and 27 in that its rate of synthesis does not decline rapidly when later polypeptides are produced. It is modified after synthesis in at least two steps, the second of which may require a later virus-specific polypeptide. In cells infected with HSV-2 the synthesis of a polypeptide analogous to ICP 22 could not be detected.
J Gen Virol 1980 Apr
PMID:Some characteristics of an early protein (ICP 22) synthesized in cells infected with herpes simplex virus. 624 73

The synthesis of virus polypeptides in rat XC cells infected with herpes simplex virus type 1 (HSV-1; 13VB4tsC75) was studied. At the permissive temperature the virus induced the synthesis, in a cascade fashion, of significant amounts of several early polypeptides (ICP 6, 8 and 39) and those late polypeptides that are relatively resistant to inhibition by phosphonoacetic acid in HEp2 cells (ICP 5, 11, 25, 29, 43 and 44). The infectious cycle appeared to become arrested in XC cells at about 7 to 9 h postinfection, because the relative concentrations of early and latest polypeptides labelled thereafter remained constant and the levels of several of the late virus polypeptides were severely reduced (ICP 2, 10, 24 and 26) or not synthesized at all (ICP 32, 34 and 37). When XC cells were infected at a very high m.o.i., only a small amount of virus DNA synthesis could be detected; the synthesis of cellular DNA was not impaired and the infected XC cells continued to replicate for several weeks at least. When XC cells were infected at the non-permissive temperature, only the immediate-early (IE) ICP 4 could be detected while IE ICP 0 and 22 were not observed. Infection of XC cells with HSV-1 (MP) also resulted in the production of early and late viral polypeptides. On the other hand, in XC cells infected with HSV-1 (F) and HSV-1 (HFEM), the synthesis of virus polypeptides could not be detected.
J Gen Virol 1983 Jul
PMID:Virus polypeptide synthesis induced by herpes simplex virus in non-permissive rat XC cells. 630 50

Cells were infected with herpes simplex virus type 2, HSV-2(G), and incubated in the presence of cycloheximide (CX). When CX was removed and actinomycin D (Act D) added, alpha-polypeptides ICP 0 and ICP 4 were synthesized at low rates. If CX was removed without adding Act D, the rate of production of ICP 4 increased while that of ICP 0 remained constant. In cells treated with azetidine to enhance the production of ICP 4 and 0, accumulation of functional mRNA for ICP 4 (determined indirectly by translation in vivo) was reduced by concentrations of CX between 0.5 and 5.0 micrograms/ml, whereas mRNA for ICP 0 was unaffected by 50 micrograms/ml CX. CX apparently either inhibits the synthesis of ICP 4 mRNA or enhances its inactivation without affecting the production or degradation of ICP 0 mRNA. The accumulation of ICP 4 or ICP 0 mRNA of HSV-1(F) was unaffected by CX. The low levels of ICP 4 and ICP 0 mRNAs of HSV-2(G) that accumulated in the presence of CX disappeared rapidly after adding Act D, in contrast to those of HSV-1(F) which were stable. The ICP 4 mRNA of HSV-2(G) was stable, however, if made without CX or if in mixed infection with HSV-1(F) in the presence of CX. It is suggested that rapid inactivation may account for the low level of accumulation of functional ICP 4 and ICP 0 mRNAs of HSV-2(G) in the presence of CX, and that ICP 4 mRNA is protected by a protein made soon after normal infection. Such a protein may be carried in the virion of HSV-1(F).
J Gen Virol 1983 Sep
PMID:The effect of cycloheximide on the accumulation and stability of functional alpha-mRNA in cells infected with herpes simplex virus. 631 35


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