The Epstein-Barr Virus (EBV) gN Homolog BLRF1 Encodes a 15-Kilodalton Glycoprotein That Cannot Be Authentically Processed unless It Is Coexpressed with the EBV gM Homolog BBRF3

Lake, Cathleen M.; Molesworth, Sara J.; Hutt-Fletcher, Lindsey

doi:10.1128/jvi.72.7.5559-5564.1998

Cited by 56 publications

(8 citation statements)

References 30 publications

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“…The meaning of this interaction is not yet fully understood but it is important for the transport of gM into the trans-Golgi-network, and only the mature gM is fully functional . Similar complex formations between gM and the respective UL49?5 products have been described for PRV, bovine herpesvirus 1 (BoHV-1), Epstein-Barr virus and human cytomegalovirus (Jöns et al, 1998;Lake et al, 1998;Wu et al, 1998;Mach et al, 2000). In most herpesviruses analysed to date, deleting gM does not result in a marked phenotype in vitro, causing its specific function still to be a matter of discussion.…”

Section: Introductionmentioning

confidence: 58%

A glycoprotein M-deleted equid herpesvirus 4 is severely impaired in virus egress and cell-to-cell spread

Ziegler

Just

Lischewski

et al. 2005

Journal of General Virology

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To analyse the function of the equid herpesvirus 4 (EHV-4) glycoprotein M homologue (gM), two different mutated viruses (E4DgM-GFP and E4DgM-w) were generated. Both gM-negative EHV-4-mutants were characterized on complementing and on non-complementing cells and compared with E4RgM, a virus where gM-expression had been repaired. It was demonstrated in virus growth kinetics that deleting gM had a more dramatic influence on EHV-4 replication than expected. Extracellular infectivity was detected 9-12 h later than in EHV-4-infected Vero cells and titres were reduced up to 2000-fold. In addition, mean maximal diameters of plaques were less than 20 % of diameters of wild-type plaques. These results are in contrast to most other alphaherpesviruses, including the closely related equid herpesvirus type 1, where deletion of gM only marginally influences the ability of viruses to replicate in cell culture. Nevertheless, analysis of infected cells by electron microscopy did not reveal a specific defect for deleting gM. It was concluded that EHV-4 gM is important for more than one step in virus replication in cell culture, influencing both efficient virus egress and cell-to-cell spread.

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Section: Introductionmentioning

confidence: 58%

A glycoprotein M-deleted equid herpesvirus 4 is severely impaired in virus egress and cell-to-cell spread

Ziegler

Just

Lischewski

et al. 2005

Journal of General Virology

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“…Encoded by the UL10 gene in HSV-1, gM is a type III membrane protein with eight predicted transmembrane domains (Baines & Roizman, 1993;MacLean et al, 1991MacLean et al, , 1993. In several herpesviruses, gM has been shown to form a disulphide-linked complex with glycoprotein N (gN), although an interaction between HSV-1 gM and gN has yet to be demonstrated (Jöns et al, 1998;Koyano et al, 2003;Lake et al, 1998;Lipiń ska et al, 2006;Mach et al, 2000;Rudolph et al, 2002;Wu et al, 1998). It has been reported that gM is non-essential for the replication of many alphaherpesviruses, including HSV-1 (Baines & Roizman, 1991;MacLean et al, 1993), pseudorabies virus (PRV) (Dijkstra et al, 1996), bovine herpesvirus type 1 (König et al, 2002), varicella-zoster virus (Yamagishi et al, 2008), infectious laryngotracheitis virus (Fuchs & Mettenleiter, 1999), equine herpesvirus type 1 (EHV-1) (Osterrieder et al, 1996) and EHV type 4 (Ziegler et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Glycoprotein M is important for the efficient incorporation of glycoprotein H–L into herpes simplex virus type 1 particles

Ren

Bell

Zenner

et al. 2012

Journal of General Virology

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Herpes simplex virus type 1 glycoprotein M (gM) is a type III membrane protein conserved throughout the family Herpesviridae. However, despite this conservation, gM is classed as a non-essential protein in most alphaherpesviruses. Previous data have suggested that gM is involved in secondary envelopment, although how gM functions in this process is unknown. Using transfection-based assays, we have previously shown that gM is able to mediate the internalization and subcellular targeting of other viral envelope proteins, suggesting a possible role for gM in localizing herpesvirus envelope proteins to sites of secondary envelopment. To investigate the role of gM in infected cells, we have now analysed viral envelope protein localization and virion incorporation in cells infected with a gM-deletion virus or its revertant. In the absence of gM expression, we observed a substantial inhibition of glycoprotein H-L (gH-L) internalization from the surface of infected cells. Although deletion of gM does not affect expression of gH and gL, virions assembled in the absence of gM demonstrated significantly reduced levels of gH-L, correlating with defects of the gM-negative virus in entry and cell-to-cell spread. These data suggest an important role of gM in mediating the specific internalization and efficient targeting of gH-L to sites of secondary envelopment in infected cells.

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“…10-to 100-folddecreased virus titers. gM forms a complex with the product of the UL49.5 homologous genes, as shown for PrV (21), bovine herpesvirus 1 (53), and Epstein-Barr Virus (27). Since the UL49.5 products are glycosylated in PrV and Epstein-Barr virus, they have been designated gN.…”

mentioning

confidence: 99%

Inhibition of Virion Maturation by Simultaneous Deletion of Glycoproteins E, I, and M of Pseudorabies Virus

Brack¹,

Dijkstra²,

Granzow

et al. 1999

J Virol

135

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Glycoprotein M (gM), the product of the UL10 gene of pseudorabies virus (PrV), is one of the few nonessential glycoproteins conserved throughout the Herpesviridae. In contrast to wild-type PrV strains, the UL10 gene product of the attenuated PrV vaccine strain Bartha (PrV-Ba) is not modified by N-glycans due to a mutation in the DNA sequence encoding the consensus N-glycosylation motif. To assay function of the UL10 protein in PrV-Ba, a UL10-deletion mutant (PrV-Ba-UL10−) was isolated. Surprisingly, in contrast to gM-deleted wild-type PrV, PrV-Ba-UL10− was severely impaired in plaque formation, inducing only foci of very few infected RK13, Vero, and PSEK cells and tiny plaques on MDBK cells. Since this effect was significantly more dramatic than in wild-type PrV, additional mutations known to be present in PrV-Ba were analyzed for their contribution to this phenotype.trans-complementation of the mutated PrV-Ba UL21 or gC protein by the wild-type version had no influence on the observed phenotype. In contrast, complementation of the gE/gI deletion rescued the phenotype. The synergistic effect of deletions in gE/gI and gM on plaque size was verified by construction of a gE/I/M triple mutant derived from wild-type PrV which exhibited the same phenotype. The dramatic effect of deletion of gM on plaque size in a gE/I− virus background was mainly attributable to a function of gM, and not of the gM/gN complex, as shown by analysis of a gE/I/N triple mutant. Interestingly, despite the strong effect on plaque size, penetration was not significantly impaired. In noncomplementing cells infected with the gE/I/M triple mutant, electron microscopy showed absence of secondary envelopment in the cytoplasm but occurrence of intracytoplasmic accumulations of nucleocapsids in association with electron dense material, presumably tegument proteins. These structures were not observed after infection of cells expressing either gE/I or gM. We suggest that gE/I and gM are required for late stages in virion morphogenesis prior to final envelopment in the cytoplasm.

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The Epstein-Barr Virus (EBV) gN Homolog BLRF1 Encodes a 15-Kilodalton Glycoprotein That Cannot Be Authentically Processed unless It Is Coexpressed with the EBV gM Homolog BBRF3

Cited by 56 publications

References 30 publications

A glycoprotein M-deleted equid herpesvirus 4 is severely impaired in virus egress and cell-to-cell spread

A glycoprotein M-deleted equid herpesvirus 4 is severely impaired in virus egress and cell-to-cell spread

Glycoprotein M is important for the efficient incorporation of glycoprotein H–L into herpes simplex virus type 1 particles

Inhibition of Virion Maturation by Simultaneous Deletion of Glycoproteins E, I, and M of Pseudorabies Virus

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