Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.1.21 (thymidine kinase)
7,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A homologue to the glycoprotein H (gH) gene of herpes simplex virus (HSV) has been identified in the genome of infectious bovine rhinotracheitis virus (IBR, BHV-1). The gene is located immediately downstream from the thymidine kinase gene, and codes for an open reading frame (orf) of 842 amino acids. The orf has the characteristics of a membrane glycoprotein, including an N-terminal hydrophobic region resembling a signal sequence, a C-terminal region which is probably a transmembrane domain, and six potential sites for N-linked glycosylation. This orf shows significant homology to the gH sequences of both HSV and pseudorabies virus (PRV). We conclude that this gene encodes BHV-1 gH.
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PMID:Cloning and sequence of an infectious bovine rhinotracheitis virus (BHV-1) gene homologous to glycoprotein H of herpes simplex virus. 165 87

The relative stability of herpes simplex virus type 1 mRNAs was investigated by examination of the decay rates of selected viral transcripts. The synthesis of mRNA was inhibited by the addition of dactinomycin to HSV-1 infected cells, and the abundance of individual transcripts was determined at subsequent times by RNA blot hybridization. For two immediate-early mRNAs, those encoding the 110 and 63 kilodalton immediate-early proteins, RNA synthesis was inhibited at 3 h post-infection and mRNA half-lives of 5-7 h were found. Examination at 5 h post-infection of the early mRNA encoding thymidine kinase as well as the late mRNA encoding glycoprotein H revealed half-lives of 8-11 h. In contrast, at 12 h post-infection, the late mRNAs encoding the glycoproteins C, E, as well as H were found to have half-lives of 14-29 h. These findings suggest that the relative stability of viral mRNA increases late in infection and is dependent upon the time after infection rather than being strictly a property of the mRNA itself.
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PMID:The relative stability of selected herpes simplex virus type 1 mRNAs. 165 58

Sequence analysis of the vaccinia virus strain Western Reserve genome revealed the presence of an open reading frame (ORF), SalL4R, which has the potential to encode a transmembrane glycoprotein with homology to C-type animal lectins (G. L. Smith, Y. S. Chan, and S. T. Howard, J. Gen. Virol. 72:1349-1376, 1991). Here we show that the SalL4R gene is transcribed late during infection from a TAAATG motif at the beginning of the ORF. Antisera raised against a TrpE-SalL4R fusion protein identified three glycoprotein species of Mr 22,000 to 24,000 in infected cells. Immunogold electron microscopy demonstrated that SalL4R protein is present in purified extracellular enveloped virus particles but not in intracellular naked virus (INV). A mutant virus was constructed by placing a copy of the SalL4R ORF downstream of an isopropyl-beta-D-thiogalactopyranoside (IPTG)-inducible vaccinia virus promoter within the thymidine kinase locus and subsequently deleting the endogenous SalL4R gene. The growth kinetics of this virus demonstrated that SalL4R was nonessential for the production of infectious INV but was required for virus dissemination. Consistent with this finding, the formation of wild-type-size plaques by this mutant was dependent on the presence of IPTG. Electron microscopy showed that without SalL4R expression, the inability of the virus to spread is due to a lack of envelopment of INV virions by Golgi-derived membrane, a morphogenic event required for virus egress.
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PMID:Identification and characterization of an extracellular envelope glycoprotein affecting vaccinia virus egress. 173 4

In-frame codon insertion and deletion mutants were constructed in a plasmid containing the sequence that encodes ICP0, a transcriptional activator of herpes simplex virus type 1 (HSV-1). The effect of these mutations was analyzed in a transient expression assay using the promoters for, the IE-0 gene (an immediate early (alpha) gene), the thymidine kinase gene (an early (beta) gene), and the glycoprotein C gene (a late (gamma) gene) fused to reporter cassettes that encoded either beta-galactosidase or chloramphenicol acetyl transferase. Assays were performed in the presence or absence of a plasmid encoding ICP4, the major regulatory protein of HSV-1. Our results demonstrate that ICP0-mediated transactivation varied depending on the position of the insertion in the gene. One region of this protein was consistently shown to be required for full activation of each promoter examined either in the presence or in the absence of ICP4. This region overlaps with a cysteine-rich region and coincides with a transactivator domain identified in another extensive mutational analysis of this sequence. Analysis of the deletion mutants generated in this study demonstrated that the carboxy-terminal regions were required for activation in certain circumstances and that this varied depending on the promoter being assayed and the cell type in which the analysis was performed.
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PMID:Mutational analysis of the sequence encoding ICP0 from herpes simplex virus type 1. 184 23

The IE-0 gene of herpes simplex virus type 1 (HSV-1) contains two introns and encodes ICP0, a powerful transcriptional activator. We have isolated a cDNA clone that encodes ICP0 from a lambda gt10 cDNA library constructed from RNAs made from HSV-1-infected HeLa cells. DNA sequence analysis of this clone confirmed the predicted intron/exon boundaries (L. J. Perry, F. J. Rixon, R. D. Everett, M. C. Frame, and D. J. McGeoch, J. Gen. Virol. 67:2365-2380, 1986). Following transfection, a plasmid containing the cDNA copy of IE-0 directed the synthesis of ICP0, which was appropriately compartmentalized and distributed in the nucleus, as revealed by immunofluorescence. A transient expression assay was used to demonstrate that this cDNA copy retained the ability to transactivate the HSV-1 promoters for the IE-0 gene (an immediate-early gene), the thymidine kinase gene (an early gene), and the glycoprotein C gene (a late gene). The product of this cDNA clone cooperated with ICP4 to activate expression from the thymidine kinase gene promoter in a synergistic manner. The availability of a functional cDNA copy encoding ICP0 provides the opportunity to express this protein in vector systems that do not recognize eucaryotic donor and acceptor splicing signals to overexpress ICP0.
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PMID:Isolation and characterization of a functional cDNA encoding ICP0 from herpes simplex virus type 1. 184 9

To investigate the cis-acting sequence elements that are involved in the regulation of herpes simplex virus type 1 late-gene expression, recombinant viruses were constructed that express the Escherichia coli lacZ gene from the promoter of the glycoprotein H (gH) gene. Deletion experiments established an upstream boundary for the gH promoter of no more than 83 bp from the start of gH transcription and showed that the promoter sequences did not overlap with coding sequences of the upstream thymidine kinase (tk) gene. Sequences of the tk gene previously shown to be required for efficient processing of the tk transcript were essential for expression form the gH promoter and included a TATA-like element. In addition, the gH TATA element was specifically mutagenized to substitute the TATA elements of immediate-early, early, and other late viral promoters for the gH TATA element. The results indicated that the TATA element was an interchangeable component of herpes simplex virus type 1 promoters and did not regulate temporal expression.
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PMID:Upstream promoter elements of the herpes simplex virus type 1 glycoprotein H gene. 184 10

A polymerase chain reaction system for the detection of varicella-zoster virus was established. Of 25 nucleotides, 4 oligonucleotide pairs (regions of thymidine kinase, thymidylate synthetase, glycoprotein I, and immediate early gene) were synthesized. The first three oligonucleotide pairs could be used as primers on the basis of specific DNA amplification. Varicella-zoster virus DNA was amplified by this polymerase chain reaction system in 20 of 20 vesicle samples, 5 of 6 crusts, and 12 of 13 throat swabs collected from patients with clinical varicella.
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PMID:Detection of varicella-zoster virus (VZV) DNA in clinical samples from patients with VZV by the polymerase chain reaction. 838 18

The primary structure of glycoprotein B (gB) is conserved strongly among many members of the Herpesviridae, including some that differ vastly in their natural properties. To determine whether the structural similarity between the gBs of herpes simplex virus type 1 (HSV-1) and bovine herpesvirus type 1 (BHV-1) was reflected in functional homology, we constructed pseudodiploid HSV-1 virions which, in addition to their own gene encoding gB, also contained a gene for encoding BHV-1 gB. Two kinds of pseudodiploid viruses were constructed. In one, the coding sequences of the BHV-1 gB gene were linked to the 5' flanking sequences of the HSV-1 thymidine kinase (TK) gene. In the other, the entire BHV-1 gB gene, including its own flanking sequences, was introduced into the TK gene. In cells infected with the viruses both HSV-1 and BHV-1 gB were made but they could be distinguished immunologically by monoclonal antibodies. Both glycoproteins were inserted into cellular and virion membranes but did not form oligomers with each other. A monoclonal antibody that binds to HSV-1 gB but not BHV-1 gB neutralized the parental HSV-1 and a revertant pseudodiploid virus from which the gene encoding BHV-1 gB had been excised, but was significantly less efficient at neutralizing the pseudodiploid viruses. This suggests that the BHV-1 homologue can complement the HSV-1 gB functions required for infectivity.
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PMID:Construction of herpes simplex viruses that are pseudodiploid for the glycoprotein B gene: a strategy for studying the function of an essential herpesvirus gene. 184 75

In the pseudorabies virus (PrV) genome a gene equivalent to the glycoprotein gH gene of other herpesviruses was identified and sequenced. It is located immediately downstream from the gene encoding PrV thymidine kinase within genomic BamHI fragments 11 and 16. Nucleotide sequencing allowed deduction of the amino acid sequence of gH. The primary translation product is predicted to comprise 686 amino acids and to exhibit a molecular weight of 71.9 kDa. It possess several characteristics typical for membrane glycoproteins, including a N-terminal hydrophobic signal sequence, C-terminal transmembrane and cytoplasmic domains, and domains with high surface probability containing three potential N-linked glycosylation sites. Comparison to other herpesvirus gH proteins revealed amino acid sequence homologies varying from 39% to gH (BHV-1), 28% to gH (HSV-1), and 19% to gH (EBV). Transcriptional analysis revealed a 2.3-kb mRNA as the gH-specific transcript. In vitro translation of either in vitro transcribed or hybrid-selected mRNA confirmed both the location of the gH gene and the size of the gH primary translation product (pgH).
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PMID:Sequence and expression of the glycoprotein gH gene of pseudorabies virus. 185 Sep 25

The Spike (S) protein from a virulent British field isolate of porcine transmissible gastroenteritis virus (TGEV) FS772/70 was constructed from cDNA and inserted into the vaccinia virus (VV) thymidine kinase gene locus under the control of the VV early/late gene P7.5k promoter. Recombinant S protein was synthesized as an endo-beta-N-acetylglucosaminidase H (Endo H)-sensitive glycoprotein with high mannose simple oligosaccharides (gp 190) that underwent post-translational modification to an Endo H-resistant glycoprotein with complex oligosaccharides (gp210). Immunofluorescence analysis demonstrated that the majority of recombinant S protein was retained at the Golgi but some S protein was expressed on the plasma membrane. Monoclonal antibodies (mAbs) raised against native S protein reacted with this recombinant S protein; also, mice infected with the recombinant vaccinia virus (rVV) expressing the S protein induced TGEV neutralizing antibodies. A truncated S protein (S delta) was also expressed in rVV-infected cells by introducing a deletion into the S protein cDNA that removed 292 amino acids from the C-terminus. The S delta protein (gp 170) was shown to be antigenically similar to TGEV S protein by immunofluorescence and immunoprecipitation tests but was retained in the endoplasmic reticulum and not expressed on the cell surface.
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PMID:Intracellular processing of the porcine coronavirus transmissible gastroenteritis virus spike protein expressed by recombinant vaccinia virus. 185 Sep 27


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