Characterization of the UL10 gene product of herpes simplex virus type 1 and investigation of its role in vivo

MacLean, Christine A.; Robertson, L M; Jamieson, Fiona E.

doi:10.1099/0022-1317-74-6-975

Cited by 66 publications

(58 citation statements)

References 27 publications

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“…gB, gH and gL are necessary for productive replication in all viruses analysed in this respect. In contrast, gM is dispensable for replication of herpes simplex virus 1 (HSV-1 ; Baines & Roizman, 1991MacLean et al, 1991MacLean et al, , 1993, equine herpesvirus 1 (Osterrieder et al, 1996) and PrV (Dijkstra et al, 1996). In these viruses, lack of gM resulted in a decrease of replicative ability in cell culture represented by 10-to 50-fold lower virus titres, a delay in entry into target cells, and slightly reduced plaque size.…”

Section: The Alphaherpesvirus Pseudorabies Virus (Prv) Causesmentioning

confidence: 99%

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Deletion of glycoprotein gM of pseudorabies virus results in attenuation for the natural host.

Dijkstra

Gerdts

Klupp

et al. 1997

Journal of General Virology

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Glycoprotein M (gM) is one of the very few nonessential glycoproteins conserved throughout the herpesvirus family. Despite this conservation little is known about its function in virus replication. To test for the importance of gM in vivo in a natural virus-host system, 6-week-old piglets were intranasally infected with a gM N mutant of the alphaherpesvirus pseudorabies virus (PrV). Following infection virus excretion from the nasal mucosa was decreased ca. 100-fold compared to wild-type or revertant virus. Clinical signs were limited to transiently elevated temperature. In contrast, animals infected by wild-type or revertant virus exhibited high fever, severe respiratory symptoms and affliction of the central nervous system. Prior infection with gM N PrV conferred protection against challenge infection and animals mounted an antibody response against gM after wild-type virus infection. Thus, gM is important for efficient virus replication in vivo and deletion of gM may contribute to development of live attenuated, genetically marked vaccines.

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Section: The Alphaherpesvirus Pseudorabies Virus (Prv) Causesmentioning

confidence: 99%

“…So far, only one investigation has dealt with growth properties of a herpesvirus gM − mutant in animals (MacLean et al, 1993). gM − HSV-1, after footpad inoculation into mice, was impaired in its ability to grow at the periphery, and spread to the nervous system.…”

Section: The Alphaherpesvirus Pseudorabies Virus (Prv) Causesmentioning

confidence: 99%

Deletion of glycoprotein gM of pseudorabies virus results in attenuation for the natural host.

Dijkstra

Gerdts

Klupp

et al. 1997

Journal of General Virology

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“…Surprisingly, the homologous proteins in herpes simplex virus type 1 (HSV-1 ; R. Adams, C. Liang et al, 1996) are not glycosylated which raises the question of importance of glycosylation for function of the protein (Paulson, 1989). gM, the product of the nonessential UL10 gene (Baines & Roizman, 1991MacLean et al, 1991MacLean et al, , 1993, is glycosylated in HSV-1 (Baines & Roizman, 1993), equine herpesvirus 1 (EHV-1 ; Osterrieder et al, 1996) and PrV (Dijkstra et al, 1996). However, the attenuated PrV strain Bartha (PrV-Ba) expresses a nonglycosylated gM (Dijkstra et al, 1997) due to a point mutation in the DNA sequence specifying the sole conserved consensus motif for Nglycan addition in gM.…”

mentioning

confidence: 99%

Different point mutations within the conserved N-glycosylation motif of pseudorabies virus glycoprotein M result in expression of a nonglycosylated form of the protein.

Dijkstra

Brack

Jöns

et al. 1998

Journal of General Virology

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Glycoprotein M (gM) constitutes one of the rare examples of a nonessential glycoprotein conserved throughout all herpesvirus subfamilies. Whereas gM in wild-type pseudorabies virus (PrV) strains carries an N-glycan, gM of the attenuated strain Bartha is not glycosylated due to a point mutation in the N-glycosylation motif. Since PrV Bartha lacks glycoproteins E and I and carries a mutated gC, we analysed glycosylation of gM in isogenic PrV glycoprotein deletion mutants. Whereas gM was glycosylated normally in most mutants, two independent gC deletion mutants and a gI mutant expressed a nonglycosylated form of gM. DNA sequence analyses revealed the presence of point mutations in the N-glycosylation consensus motif. Surprisingly, mutations in strain Bartha, the two gCdeletion mutants and the gI mutant proved to be different, although all affected the N-glycosylation motif. Thus, our data show that different, apparently independent point mutations cause expression of nonglycosylated gM.In pseudorabies virus (PrV), a member of the alphaherpesvirus subfamily of the herpesviruses, 11 glycoproteins have been described up to now (reviewed in Mettenleiter, 1994). They include homologues of the essential gB, gH and gL, and the nonessential gM and gN, which are found in all herpesvirus subfamilies. Conservation of glycoproteins apparently not required for productive replication of the virus, at least in cell culture, appears to be rare and most nonessential glycoproteins detected in alphaherpesviruses are not present in beta-or gammaherpesviruses. We recently identified the product of the UL49.5 open reading frame of PrV as an Oglycosylated virion envelope component designated gN (Jo$ ns

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“…Especially, the protein encoded by the HSV-1 UL10 gene is predicted to contain eight transmembrane domains and has recently been described as a N-glycosylated component of the virion designated gM [4,26]. The only nonessential glycoprotein conserved throughout the Herpesviridae family is gM [3,26]. The gM homologue was first identified in human cytomegalovirus (HCMV) as integral membrane protein, a 45 kDa structural component of the virion [24].…”

mentioning

confidence: 99%

“…The HSV-1 genome contains four genes, UL10, UL20, UL43, and UL53, which are predicted to encode hydrophobic proteins with the potential to pass the membrane several times [28]. Especially, the protein encoded by the HSV-1 UL10 gene is predicted to contain eight transmembrane domains and has recently been described as a N-glycosylated component of the virion designated gM [4,26]. The only nonessential glycoprotein conserved throughout the Herpesviridae family is gM [3,26].…”

mentioning

confidence: 99%

Identification and Structure of the Marek's Disease Virus Serotype 2 Glycoprotein M Gene: Comparison with Glycoprotein M Genes of Herpesviridae Family

Cai

Jang

Izumiya

et al. 1999

The Journal of Veterinary Medical Science

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ABSTRACT. We determined the nucleotide sequence of a portion of BamHI-C fragment of Marek's disease virus serotype 2 (MDV2) strain HPRS24 which was suspected to contain the homologue of the herpes simplex virus type 1 (HSV-1) gene UL10, encoding glycoprotein M (gM). An open reading frame whose translation product exhibited significant similarities to HSV-1 gM protein and respective proteins of other herpesviruses of 37.5% and 45.5% to 31.8%, respectively, was identified. A number of distinct transcriptional consensus sequences were found upstream of the first putative start codon of MDV2 UL10 protein. In transcriptional analysis, the gene was transcribed into an 1.5 kb RNA. The primary translation product comprises 424 amino acids with a predicted molecular weight of 46.9 kDa. The predicted MDV2 UL10 protein contains eight hydrophobic domains with sufficient length and hydrophobicity to span the lipid bilayer conserved in the genomes of all herpesviruses which have been sequenced so far. In the region located between the first and second hydrophobic domains, two potential N-linked glycosylation sites were presented. Interestingly, highly charged residues were abundantly possessed in the carboxy-terminal part of the MDV2 UL10 protein. By comparison of the amino acid sequence of the MDV2 UL10 gene with the homologues from other herpesviruses, the data might contribute for further evidence of the evolution of herpesviruses from a common progenitor and an ancient example of MDV2 belonging to the Alphaherpesvirinae subfamily. In addition, the existence of corresponding genes in human, mammalian, and avian herpesvirus genomes, suggests indirectly an important role for gM in the natural life cycle of the virus.-KEY WORDS: gM, MDV, MDV2, UL10.J. Vet. Med. Sci. 61(5): 503-511,1999 throughout the Herpesviridae family, including homologues of herpes simplex virus type 1 (HSV-1) gB, gH, gL, and gM, and so far, others, such as gC, gD, gE, gG, gI and gK, are found only in the Alphaherpesvirinae subfamily [39].

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Characterization of the UL10 gene product of herpes simplex virus type 1 and investigation of its role in vivo

Cited by 66 publications

References 27 publications

Deletion of glycoprotein gM of pseudorabies virus results in attenuation for the natural host.

Deletion of glycoprotein gM of pseudorabies virus results in attenuation for the natural host.

Different point mutations within the conserved N-glycosylation motif of pseudorabies virus glycoprotein M result in expression of a nonglycosylated form of the protein.

Identification and Structure of the Marek's Disease Virus Serotype 2 Glycoprotein M Gene: Comparison with Glycoprotein M Genes of Herpesviridae Family

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