Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids

Addison, Caroline; Rixon, Frazer J.; Palfreyman, John W.; O’Hara, Maureen; Preston, Valerie G.

doi:10.1016/0042-6822(84)90349-0

Cited by 99 publications

(71 citation statements)

References 33 publications

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“…3(b). A somewhat stronger affinity was noted for HSV-2 with more efficient binding, but it seems doubtful that this discrepancy would be sufficiently large to explain the observed differences in receptor affinity (Addison et al, 1984;Vahlne et al, 1979) and sensitivity to competition by polycationic compounds (Langeland et al, 1988). However, as pointed out first by WuDunn & Spear (1989), attachment to heparan sulphate probably represents only the initial step in the anchoring of the virion to the plasma membrane.…”

Section: Discussionmentioning

confidence: 87%

“…Whether HSV-1 and HSV-2 interfere with each other at the cell surface level has been a matter of debate (Addison et al, 1984;Langeland et al, 1988;Vahlne et al, 1979;WuDunn & Spear, 1989) and it has not been determined whether the two types utilize the same or different receptor structures. Both HSV-1 and HSV-2 bind to heparan sulphate (WuDunn & Spear, 1989), but whereas neomycin reversibly blocks the binding of HSV-1 to cells, the attachment of HSV-2 is unaffected (Langeland et al, 1988), suggesting typespecific differences in the interactions of the virus and its cellular receptors.…”

Section: Introductionmentioning

confidence: 99%

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Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Lycke

Johansson²,

Svennerholm³

et al. 1991

Journal of General Virology

135

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It has been suggested that heparan sulphate has a receptor function in the initial phase of the attachment of herpes simplex virus (HSV) to cells. We have studied the influence of glycosaminoglycans on cell adsorption of, and plaque formation by, HSV-1 and HSV-2, with regard to the role of saccharide structure, chain length and charge density. Heparin and highly-sulphated heparan sulphate (1-5 sulphate groups/disaccharide unit), but neither chondroitin sulphate nor dermatan sulphate, were found to compete with the cellular receptor for attachment of HSV. Heparan sulphate preparations of low sulphate content (0.5 and 0.7 sulphate groups/disaccharide unit) failed to show any significant interaction with HSV. Oligosaccharides generated by partial deaminative cleavage of heparin were used to determine the minimum molecular size required for the binding of virus; the smallest oligosaccharide which reacted with HSV was composed of l0 monosaccharide units. The importance of charge density was demonstrated more directly by subfractionation of the heparin dodecasaccharide fraction by anion-exchange HPLC. The virus-binding capacities of the four resulting dodecasaccharide subfractions increased from the least sulphated to the most heavily sulphated fraction. The results reported are discussed in relation to virus-receptor interactions involved in the attachment of HSV, including the reported binding of HSV to the fibroblast growth factor receptor.

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Section: Discussionmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Lycke

Johansson²,

Svennerholm³

et al. 1991

Journal of General Virology

135

View full text Add to dashboard Cite

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“…The localization of TK was clearly different from that observed for DNA-binding proteins (e.g. Addison et al, 1984). At the highest dilution of antiserum, the fluorescence revealed a preferential perinuclear distribution (Fig.…”

Section: Subcellular Localization Of Tk and Ability To Bind To Dnamentioning

confidence: 88%

“…Cells were grown on coverslips, infected for 5, 6 or 12 h, fixed overnight in methanol at -20 °C and stored at 4 °C in PBS containing 0-1 ~ sodium azide (Norrild et al, 1986). Preincubation with normal rabbit serum was carried out for 1 h at room temperature (Addison et al, 1984) followed by incubation overnight at 4 °C with a dilution of antiserum. FITC-coupled antibody was diluted 1 : 20 with PBS, added to the cells and allowed to act for 1 h at room temperature.…”

Section: Measurement Of Proteinmentioning

confidence: 99%

Evidence that Deletion of Coding Sequences in the 5' End of the Thymidine Kinase Gene of Herpes Simplex Virus Type 1 Affects the Stability of the Gene Products

Haarr

Flatmark²

1987

Journal of General Virology

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SUMMARYThe experiments described in the present work were designed to study the function of the N-terminal end of thymidine kinase (TK) encoded by herpes simplex virus type 1. Specifically we were interested to know whether this end was involved in binding of the enzyme to other molecules, had any influence on its subcellular localization or affected one or more of the activities associated with the enzyme. A parental enzyme and a deletion mutant, lacking the 45 N-terminal amino acids, derived from this strain, were used. Thymidine kinase from the parental virus bound to DNA-Sepharose, but the truncated enzyme did not. This was apparently not due to a specific ability to bind to DNA, since immunofluorescence studies indicated that both the normal and the deleted TK were mainly located in the cytoplasm, preferentially in the perinuclear region. Phosphorylation of thymidine as well as the amounts of TK potypeptides were markedly reduced at late times after infection with the mutant, but not to the same extent after infection with the wild-type. The deleted TK gene was efficiently transcribed as shown by hybridization of RNA to a probe specific for the gene, and this RNA directed the synthesis in vitro of TK polypeptides. Deletion of the 5' end of the gene seems to affect the stability of either the enzyme or TK-specific mRNA, or both. The TMP phosphorylating activity seems to be particularly destabilized relative to the thymidine phosphorylating activity.

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“…that products of the UL28 gene, together with those of UL6, UL25, UL32 and UL33 genes, are required for formation of full capsids, for packaging of viral DNA and for expression of viral glycoproteins on the surface of virus-infected cells [1,2,32]. The MDV2 putative UL29 gene contains 3,573 bp ORF encoding 1,190 amino acids.…”

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confidence: 99%

Identification of the Marek’s Disease Virus Serotype 2 Genes Homologous to the Glycoprotein B (UL27), ICP18.5 (UL28) and Major DNA-Binding Protein (UL29) Genes of Herpes Simplex Virus Type 1

Kato

Jang

Izumiya

et al. 1999

The Journal of Veterinary Medical Science

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ABSTRACT. We determined the nucleotide sequence of non-pathogenic Marek's disease virus serotype 2 (MDV2) strain HPRS24 glycoprotein B (gB) (UL27), ICP18.5 (UL28) and major DNA-binding protein (MDBP) (UL29) genes homologous to herpes simplex virus type 1 (HSV-1). The sequence data revealed that important motives in the proteins are conserved in MDV2 ICP18.5 and MDBP, however the sequence of viral DNA replication origin which exists in the regions between the UL29 and UL30 genes of other alphaherpesviruses was not found in the regions of the MDV2 genome. By northern blot analyses, we also demonstrated that 8.9, 5.0 and 2.6 kb transcripts were actually transcribed from the sequenced region in MDV2-infected cells. 1B) were then deleted by exonuclease III to construct deletion clones. After that DNA sequences were determined on both strands using an autosequencer system (Applied Biosystems, Foster City, CA). DNA and amino acid sequences were analyzed with the computer program GENETYX-MAC (version 8.0). Homology searches and multiple sequence alignments from the GenBank and EMBL Data Libraries were performed using the UWGCG programs BESTFIT and PILEUP, respectively. The nucleotide sequences of the MDV2 UL27, UL28 and UL29 homologues have been submitted to the DDBJ, EMBL and GenBank Databanks with the Accession No. AB024711.The location of the MDV2 (HPRS24 strain) UL27, UL28 and UL29 homologues in virus genome, pertinent restriction endonuclease sites are illustrated in Fig. 1. We determined the nucleotide sequence of a total of 9,650 bp containing the putative sequences of MDV2 UL27, UL28 and UL29 homologues of the HSV-1 gene (Fig. 1C).To find out whether transcripts are really transcribed from the domain of MDV2 genome containing the identified genes of MDV2 UL27, UL28, and UL29, northern blot analyses were performed using the different probes. The maintenance of primary chicken embryo fibroblasts (CEF) and infection of CEF with MDV2 strain HPRS24 were performed as described previously [14]. To isolate total RNA, monolayers were harvested at 96 hr postinfection and treated with 0.05% ethylenediaminetetraacetic acid in phosphate-buffered saline. Total RNAs were extracted from these lysates by ISOGEN (Nippon Gene, Tokyo, Japan). Total RNA was separated on an agarose formaldehyde-gel Marek's disease virus (MDV) is a cell-associated alphaherpesvirus of poultry and causes a naturally occurring malignant T cell lymphoma in chickens. The virus is divided into three serotypes.They belong to alphaherpesviruses, based on their genomic structures and arrangements [4,11,21]. The disease can be prevented by vaccination with attenuated MDV serotype 1 (MDV1), nonpathogenic MDV serotype 2 (MDV2) or herpesvirus of turkeys (HVT) known as a MDV serotype 3 (MDV3). The MDV2 genome differs in restriction endonuclease digestion patterns from those of either MDV1 or HVT [10,25,30]. However, information about the genomic analysis of MDV2 is limited and only the genes encoding for glycoproteins gB (SB-1 strain) [34] [22] have been reported....

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Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids

Cited by 99 publications

References 33 publications

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Evidence that Deletion of Coding Sequences in the 5' End of the Thymidine Kinase Gene of Herpes Simplex Virus Type 1 Affects the Stability of the Gene Products

Identification of the Marek’s Disease Virus Serotype 2 Genes Homologous to the Glycoprotein B (UL27), ICP18.5 (UL28) and Major DNA-Binding Protein (UL29) Genes of Herpes Simplex Virus Type 1

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Characterisation of a herpes simplex virus type 1 mutant which has a temperature-sensitive defect in penetration of cells and assembly of capsids

Cited by 99 publications

References 33 publications

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Binding of herpes simplex virus to cellular heparan sulphate, an initial step in the adsorption process

Evidence that Deletion of Coding Sequences in the 5' End of the Thymidine Kinase Gene of Herpes Simplex Virus Type 1 Affects the Stability of the Gene Products

Identification of the Marek&rsquo;s Disease Virus Serotype 2 Genes Homologous to the Glycoprotein B (UL27), ICP18.5 (UL28) and Major DNA-Binding Protein (UL29) Genes of Herpes Simplex Virus Type 1

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Identification of the Marek’s Disease Virus Serotype 2 Genes Homologous to the Glycoprotein B (UL27), ICP18.5 (UL28) and Major DNA-Binding Protein (UL29) Genes of Herpes Simplex Virus Type 1