Expression of Bovine Herpesvirus Type 1 Glycoprotein gI in Transfected Bovine Cells Induces Spontaneous Cell Fusion

FitzPatrick, David R.; Zamb, Timothy J.; Babiuk, Lorne A.

doi:10.1099/0022-1317-71-5-1215

Cited by 28 publications

(25 citation statements)

References 8 publications

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“…The fusion function ofgI may be species-specific as the gI gene used in our studies was the same as that used by Fitzpatrick et al, 1988b) when they observed polykaryon formation in gl-expressing murine cells.…”

Section: Short Communicationmentioning

confidence: 94%

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Chase

Carter-Allen²,

Letchworth³

1989

Journal of General Virology

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SUMMARYWe expressed the bovine herpesvirus type 1 (BHV-1) glycoproteins, gI and gIII, in bovine cells using a bovine papillomavirus vector. The proteins expressed by these cells had the same Mr as the native BHV-1 proteins and monoclonal antibodies detected no differences in their antigenic structure. Cells expressing gI were infected with either BHV-1 or herpes simplex virus type 1 (HSV-1). The number of plaques in gI-expressing cells was similar to that seen with normal fibroblasts infected with BHV-1 or HSV-1. However, BHV-1 or HSV-1 plaques produced in gI-expressing cells were smaller and darker than those seen in normal fibroblasts indicating an interference with cell-to-cell transmission or cellular lysis. Virus growth curves and [3SS]methionine labelling of BHV-l-infected gI-expressing cells showed no difference in virus production, virus protein synthesis or cellular protein shutdown when compared to BHV-l-infected normal cells. This led us to conclude that the gI protein may interfere with a cellular protein(s) responsible for the cytopathic effects of BHV-1 infection. Cells expressing gIII were fully susceptible to BHV-1 infection.

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Section: Short Communicationmentioning

confidence: 94%

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Chase

Carter-Allen²,

Letchworth³

1989

Journal of General Virology

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“…When HSVgB is expressed in mammalian cells it causes considerable cell membrane fusion resulting in syncytium formation (Ali et al, 1987). BHVgB expressed in mammalian cells also displays similar membranefusing abilities (Fitzpatrick et al, 1988). In recombinant pseudodiploid HSV which expresses both glycoproteins, BHVgB can complement an essential function of HSVgB which has been blocked by a neutralizing monoclonal antibody (MAb) H233 (Misra & Blewett, 1991).…”

Section: Introductionmentioning

confidence: 99%

Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function

Blewett

Misra

1991

Journal of General Virology

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Herpes simplex virus glycoprotein B (HSVgB) and its bovine herpesvirus homologue (BHVgB) share similar primary structures. These glycoproteins are present in the envelope of the virion and are believed to initiate infection by fusing the virus envelope with a host cell membrane. BHVgB, like the membrane-fusing glycoproteins of most enveloped viruses, is normally cleaved and is present as a disulphide-linked complex in the virus envelope and host cell membranes. HSVgB, however, remains uncleaved, presumably because it lacks a similar protease recognition sequence. To determine whether the cleavage of BHVgB is essential for its role in initiating infection, we altered the coding sequence of this glycoprotein by removing the protease cleavage site and making this region similar to that of HSVgB. The mutant BHVgB gene was expressed by an HSV recombinant virus in mouse L cells and produced an uncleaved BHVgB. The uncleaved BHVgB could complement the function of HSVgB which had been neutralized by monoclonal antibody H233. When expressed in mouse L cells, the uncleaved mutant BHVgB retained its ability to fuse membranes.

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“…gB is the most conserved glycoprotein, with its function as a fusion protein well documented for several of the herpesviruses (10,19,38,48,51,52).…”

mentioning

confidence: 99%

Mutagenesis of Varicella-Zoster Virus Glycoprotein B: Putative Fusion Loop Residues Are Essential for Viral Replication, and the Furin Cleavage Motif Contributes to Pathogenesis in Skin Tissue In Vivo

Oliver

Sommer

Zerboni

et al. 2009

J Virol

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Glycoprotein B (gB), the most conserved protein in the family Herpesviridae, is essential for the fusion of viral and cellular membranes. Information about varicella-zoster virus (VZV) gB is limited, but homology modeling showed that the structure of VZV gB was similar to that of herpes simplex virus (HSV) gB, including the putative fusion loops. In contrast to HSV gB, VZV gB had a furin recognition motif ([R]-X-[KR]-R-ͦ-X, where ͦ indicates the position at which the polypeptide is cleaved) at residues 491 to 494, thought to be required for gB cleavage into two polypeptides. To investigate their contribution, the putative primary fusion loop or the furin recognition motif was mutated in expression constructs and in the context of the VZV genome. Varicella-zoster virus (VZV), an alphaherpesvirus, causes chicken pox (varicella) as a primary infection and shingles (zoster) upon reactivation from infected ganglia in humans (reviewed in reference 16).Although not yet investigated in VZV, herpesvirus entry requires fusion of the virus envelope with cell membranes governed by viral glycoprotein B (gB) and gH/gL, which are conserved across the family Herpesviridae (12,27,57). gB is the most conserved glycoprotein, with its function as a fusion protein well documented for several of the herpesviruses (10,19,38,48,51,52).Open reading frame 31 (ORF31) codes for the 931 amino acids of VZV gB (18, 37). The successive N-and O-linked glycosylation plus the sialation and sulfation of VZV gB yields a mature protein with a molecular mass of approximately 140 kDa (45). Upon maturation, gB is cleaved, presumably by cellular proteases, into two polypeptides of 66 and 68 kDa. Intracellular trafficking of gB was shown to be dependent upon amino acid motifs in the cytoplasmic domain (24-26). In transfection studies, gB was transported to the cellular surface where it was endocytosed and localized to the trans-Golgi, where envelopment of viral particles is thought to occur.The structures of gB in the two human alphaherpesviruses, VZV and herpes simplex virus type 1 (HSV-1), are likely to be very similar as they have 49% amino acid identity (reviewed in reference 16). The ectodomain of HSV-1 gB was shown to form a spike that consisted of trimers with the structural homology to gG of vesicular stomatitis virus (28). Heldwein et al. (28) proposed that HSV-1 gB is a class II fusion protein based on homology to VSV G. The herpesvirus gB monomer was divided into five domains, I to V. Domain I consisted of a continuous amino acid sequence that folded into a pleckstrin homology-like domain, while domain II was comprised of two discontinuous segments, which also had a pleckstrin homologylike domain. A loop region exposed to the exterior of gB connected domain II with domain III. Domain III was comprised of three discontinuous segments and connected to the external loop by a long ␣ helix that ended in a central coiled coil. Domain IV crowned gB and was connected to domain V, which stretched from the top to the bottom of the gB monomer, forming ...

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Expression of Bovine Herpesvirus Type 1 Glycoprotein gI in Transfected Bovine Cells Induces Spontaneous Cell Fusion

Cited by 28 publications

References 8 publications

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

The Effect of Bovine Herpesvirus Type 1 Glycoproteins gI and gIII on Herpesvirus Infections

Cleavage of the bovine herpesvirus glycoprotein B is not essential for its function

Mutagenesis of Varicella-Zoster Virus Glycoprotein B: Putative Fusion Loop Residues Are Essential for Viral Replication, and the Furin Cleavage Motif Contributes to Pathogenesis in Skin Tissue In Vivo

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