Identification and characterization of a novel non-infectious herpes simplex virus-related particle

Szilágyi, J. F.; Cunningham, Charles

doi:10.1099/0022-1317-72-3-661

Cited by 174 publications

(163 citation statements)

References 32 publications

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“…The virus suspension was centrifuged at 1,900 x g for 5 min to remove cell debris. The resulting suspension was centrifuged at 20,000 x g for 2 hours [42]. The virus pellet was resuspended in 2ml of TE buffer.…”

Section: Virus Isolationmentioning

confidence: 99%

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Equine herpesvirus infections in yearlings in South-East Queensland

et al. 2008

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SummaryTwelve nasal swabs were collected from yearling horses with respiratory distress and tested for Equid herpesvirus 1 (EHV-1) and Equid herpesvirus 4 (EHV-4) by realtime PCR targeting the glycoprotein B gene. All samples were negative for EHV-1; however 3 were positive for EHV-4. When these samples were tested for EHV-2 and EHV-5 by PCR all samples were negative for EHV-2 and 11 were positive for EHV-5. All three samples that were positive for EHV-4 were also positive for EHV-5.These three samples gave a limited CPE in ED cells reminiscent of EHV-4 CPE.EHV-4 CPE was obvious after 3 days and was characterised by syncytia. None of the samples produced cytopathic effect (CPE) on African green monkey kidney (Vero) cells or hamster kidney (BSR) cells. Four of the samples, which were positive in the EHV-5 PCR, produced CPE on rabbit kidney (RK13) cells and equine dermis (ED) cells. EHV-5 CPE on both cell lines was slow and was apparent after four 7-day passages. On RK13 cells the CPE was characteristic of equid herpesvirus with the formation of syncytia. However in ED cells, the CPE was characterised by ringshaped syncytia.For the first time a case of equine respiratory disease involving dual infection with EHV-4 and EHV-5 has been reported in Queensland. This was shown by simultaneously isolating EHV-4 and EHV-5 from clinical samples. EHV5 was recovered from all samples except one, suggesting that EHV5 was more prevalent in young horses than EHV2.

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Section: Virus Isolationmentioning

confidence: 99%

“…The EHV-2 PCR was derived from a method described by Telford et al [42]. This was a nested PCR; however in order to decrease chances of contamination the PCR was modified to be performed as a single round PCR.…”

Section: Polymerase Chain Reactionmentioning

confidence: 99%

Equine herpesvirus infections in yearlings in South-East Queensland

et al. 2008

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“…Virion and L-particle purification. [ 35 S]methionine-labeled virions and L particles were pelleted from the extracellular medium of infected BHK-21 cells, resuspended in a small volume of MEM, and sedimented through two successive 5 to 15% Ficoll gradients prepared in MEM (74,78). Centrifugation was at 24,000 rpm for 100 min in a Beckman SW41 Ti rotor.…”

Section: Purification Of Virions and Capsids (I) Extracellular Virionsmentioning

confidence: 99%

Packaging of the Virion Host Shutoff (Vhs) Protein of Herpes Simplex Virus: Two Forms of the Vhs Polypeptide Are Associated with Intranuclear B and C Capsids, but Only One Is Associated with Enveloped Virions

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Patterson

2007

J Virol

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The virion host shutoff (Vhs) protein (UL41) is a minor component of herpes simplex virus virions which, following penetration, accelerates turnover of host and viral mRNAs. Infected cells contain 58-kDa and 59.5-kDa forms of Vhs, which differ in the extent of phosphorylation, yet only a 58-kDa polypeptide is incorporated into virions. In pulse-chase experiments, the primary Vhs translation product comigrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with the 58-kDa virion polypeptide, and could be chased to 59.5 kDa. While both 59.5-kDa and 58-kDa forms were found in nuclear and cytoplasmic fractions, the 59.5-kDa form was significantly enriched in the nucleus. Both forms were associated with intranuclear B and C capsids, yet only the 58-kDa polypeptide was found in enveloped cytoplasmic virions. A 58-kDa form, but not the 59.5-kDa form, was found in L particles, noninfectious particles that contain an envelope and tegument but no capsid. The data suggest that virions contain two populations of Vhs that are packaged by different pathways. In the first pathway, the primary translation product is processed to 59.5 kDa, is transported to the nucleus, binds intranuclear capsids, and is converted to 58 kDa at some stage prior to final envelopment. The second pathway does not involve the 59.5-kDa form or interactions between Vhs and capsids. Instead, the primary translation product is phosphorylated to the 58-kDa virion form and packaged through interactions with other tegument proteins in the cytoplasm or viral envelope proteins at the site of final envelopment.Controls of the rate of mRNA decay play an important role in eukaryotic gene expression (3, 6-9, 47, 48, 55, 66). During lytic herpes simplex virus (HSV) infections, the half-lives of host and viral mRNAs are regulated by the HSV virion host shutoff (Vhs) protein (21,34,35,52,53,56,64,73). Vhs is an endoribonuclease (12,13,16,40,41,77,87) that is a minor structural component of HSV virions (58,68) and that, following release from infecting virions, accelerates the degradation of most cellular mRNAs in the cytoplasm (21,64,73). Following the onset of viral transcription, Vhs also accelerates the turnover of viral mRNAs (34,35,52,53,73

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“…Recently the use of cryoelectron tomography has revealed the tegument as frequently forming an asymmetric cap between the capsid and outer envelope (16). The identification of cytoplasmic HSV "light particles" (26), which consist of the authentic viral membrane with a full complement of embedded glycoproteins and subjacent tegument, indicates that most of the tegument and glycoprotein can self-assemble within the cytoplasm (37). Most of the tegument proteins are present in HSV-1 light particles, including UL36 (37) and UL37 (25).…”

mentioning

confidence: 99%

Determination of Interactions between Tegument Proteins of Herpes Simplex Virus Type 1

Vittone

Diefenbach

Triffett

et al. 2005

J Virol

187

224

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The aim of this study was to elucidate protein-protein interactions between tegument proteins of herpes simplex virus type 1 (HSV-1). To do so, we have cloned and expressed in the LexA yeast (Saccharomyces cerevisiae) two-hybrid system, 13 of the 21 currently known tegument proteins of HSV-1. These included the tegument proteins essential for replication in cell lines, UL17, UL36, UL37, UL48, and UL49, and the nonessential tegument proteins US11, UL11, UL14, UL16, UL21, UL41, UL46, and UL47. A total of 104 combinations were screened in the yeast two-hybrid assay, with 9 interactions identified. These included: UL11-UL16, UL36-UL37, UL36-UL48, UL46-UL48, UL47-UL48, and UL48-UL49. The remaining interactions consisted of self-associations that were observed for US11, UL37, and UL49. The interactions UL36-UL37, UL36-UL48, UL37-UL37, UL46-UL48, and UL47-UL48 have not been previously reported for HSV-1. The interaction of UL46-UL48 was verified using an in vitro pull-down assay. The interactions of UL36-UL37 and UL37-UL37 were verified with a coimmunoprecipitation assay. Knowledge of HSV-1 tegument protein-protein interactions will provide insights into the pathways of tegument assembly, and the identified interactions are potential targets for new antiviral drugs.

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Identification and characterization of a novel non-infectious herpes simplex virus-related particle

Cited by 174 publications

References 32 publications

Equine herpesvirus infections in yearlings in South-East Queensland

Equine herpesvirus infections in yearlings in South-East Queensland

Packaging of the Virion Host Shutoff (Vhs) Protein of Herpes Simplex Virus: Two Forms of the Vhs Polypeptide Are Associated with Intranuclear B and C Capsids, but Only One Is Associated with Enveloped Virions

Determination of Interactions between Tegument Proteins of Herpes Simplex Virus Type 1

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