Three major glycoprotein genes of varicella-zoster virus whose products have neutralization epitopes

Keller, Paul M.; Neff, Beverly J.; Ellis, Ronald W.

doi:10.1128/jvi.52.1.293-297.1984

Cited by 91 publications

(38 citation statements)

References 30 publications

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“…Interestingly, a previous study by these authors showed that the smaller form of gE is present on cell surface, recycles through the endocytotic pathway, and is incorporated into virions [28]. Studies from other groups also showed that a mixture of forms of gE ranging from ,50-100 kDa are present in purified virions [29,30,31]. Therefore, the 73 kDa form of gE is present in virions where it may interact with IDE.…”

Section: Discussionmentioning

confidence: 93%

Insulin Degrading Enzyme Induces a Conformational Change in Varicella-Zoster Virus gE, and Enhances Virus Infectivity and Stability

Ali

Wang

et al. 2010

PLoS ONE

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Varicella-zoster virus (VZV) glycoprotein E (gE) is essential for virus infectivity and binds to a cellular receptor, insulin-degrading enzyme (IDE), through its unique amino terminal extracellular domain. Previous work has shown IDE plays an important role in VZV infection and virus cell-to-cell spread, which is the sole route for VZV spread in vitro. Here we report that a recombinant soluble IDE (rIDE) enhances VZV infectivity at an early step of infection associated with an increase in virus internalization, and increases cell-to-cell spread. VZV mutants lacking the IDE binding domain of gE were impaired for syncytia formation and membrane fusion. Pre-treatment of cell-free VZV with rIDE markedly enhanced the stability of the virus over a range of conditions. rIDE interacted with gE to elicit a conformational change in gE and rendered it more susceptible to proteolysis. Co-incubation of rIDE with gE modified the size of gE. We propose that the conformational change in gE elicited by IDE enhances infectivity and stability of the virus and leads to increased fusogenicity during VZV infection. The ability of rIDE to enhance infectivity of cell-free VZV over a wide range of incubation times and temperatures suggests that rIDE may be useful for increasing the stability of varicella or zoster vaccines.

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Section: Discussionmentioning

confidence: 93%

Insulin Degrading Enzyme Induces a Conformational Change in Varicella-Zoster Virus gE, and Enhances Virus Infectivity and Stability

Ali

Wang

et al. 2010

PLoS ONE

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“…were scraped from minimal lactose plates into SDSpolyacrylamide gel sample buffer, boiled, electrophoresed, transferred to nitrocellulose, and reacted with antibodies as previously described (15). Rabbit anti-beta-galactosidase antiserum (a gift from V. Larson) was prepared to E. coli beta-galactosidase (Sigma catalog no.…”

Section: Methodsmentioning

confidence: 99%

“…G-6008). The source of other ascites fluids, convalescent zoster serum, and normal human serum has been previously described (15). Southern blots.…”

Section: Methodsmentioning

confidence: 99%

“…RNA was translated in vitro in rabbit reticulocyte lysates (Bethesda Research Laboratories) according to the recommendations of the supplier. In vitro translational products were immunoprecipitated, electrophoresed, and autoradiographed as previously described (15).…”

Section: Methodsmentioning

confidence: 99%

“…Recently, we described the reactivities of monoclonal antibodies to VZV (15). In toto, these antibodies recognized eight distinct glycoprotein species in infected cells and virions.…”

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confidence: 99%

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Use of a bacterial expression vector to map the varicella-zoster virus major glycoprotein gene, gC

Ellis¹,

Keller²,

Lowe³

et al. 1985

J Virol

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The genome of varicella-zoster virus (VZV) encodes at least three major glycoprotein genes. Among viral gene products, the gC gene products are the most abundant glycoproteins and induce a substantial humoral immune response (Keller et al., J. Virol. 52:293-297, 1984). We utilized two independent approaches to map the gC gene. Small fragments of randomly digested VZV DNA were inserted into a bacterial expression vector. Bacterial colonies transformed by this vector library were screened serologically for antigen expression with monoclonal antibodies to gC. Hybridization of the plasmid DNA from a gC antigen-positive clone revealed homology to the 3' end of the VZV U,, segment. In addition, mRNA from VZV-infected cells was hybrid selected by a set of VZV DNA recombinant plasmids and translated in vitro, and polypeptide products were immunoprecipitated by convalescent zoster serum or by monoclonal antibodies to gC. This analysis revealed that the mRNA encoding a 70,000-dalton polypeptide precipitable by anti-gC antibodies mapped to the Hindlll C fragment, which circumscribes the entire U, region. We conclude that the VZV gC glycoprotein gene maps to the 3' end of the U, region and is expressed as a 70,000-dalton primary translational product. These results are consistent with the recently reported DNA sequence of Us (A.

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Neutralizing antibody responses induced by varicella-zoster virus gE and gB glycoproteins following infection, reactivation or immunization

Haumont¹,

Jurdan²,

Kangro³

et al. 1997

J. Med. Virol.

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The purpose of this study was to compare the antibody responses to varicella-zoster virus (VZV) gE and gB after natural VZV infection and after vaccination with live attenuated OKA vaccine in order to determine the relative importance of these proteins as components of a subunit vaccine. Anti-VZV antibody titers determined by IFA were of the same order of magnitude in sera from individuals with a history of varicella and in vaccinated children but higher in individuals given booster vaccination. The titers of anti-gE and anti-gB antibodies were measured by ELISA using recombinant gE or gB as capture antigen. From these experiments, it appears that the ratio of anti-gE to anti-gB antibody is highly variable from one individual to another but relatively stable over a long period of time for a particular individual, even after a zoster episode. Neutralizing antibodies directed against gE or gB were also measured by subtracting the neutralization titers obtained before and after depletion of the specific antibodies on immobilized recombinant gE, gB, or both. This showed that, with respect to neutralization, anti-gE and anti-gB are equally prevalent in vaccinated children and that anti-gE is generally, but not always, predominant over anti-gB in VZV-infected individuals. Finally, antibodies to these two glycoproteins appear to be predominant among the neutralizing antibodies directed to other VZV antigens.

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Three major glycoprotein genes of varicella-zoster virus whose products have neutralization epitopes

Cited by 91 publications

References 30 publications

Insulin Degrading Enzyme Induces a Conformational Change in Varicella-Zoster Virus gE, and Enhances Virus Infectivity and Stability

Insulin Degrading Enzyme Induces a Conformational Change in Varicella-Zoster Virus gE, and Enhances Virus Infectivity and Stability

Use of a bacterial expression vector to map the varicella-zoster virus major glycoprotein gene, gC

Neutralizing antibody responses induced by varicella-zoster virus gE and gB glycoproteins following infection, reactivation or immunization

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