Varicella-Zoster Virus Fails to Induce Immunoglobulin G Fc Receptors in Infected Human Cells

Gelb, Lawrence D.; Wellinghoff, Wanda; Martin, Joel; Huang, John J.

doi:10.3181/00379727-168-41265

Cited by 7 publications

(4 citation statements)

References 8 publications

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“…The use of heat- aggregated IgG, a more sensitive indicator of Fc receptors, also consistently failed to reveal the presence of this product in VZV-infected cells. The findings of previous work showing false-positive reactions by immunofluorescence in tests for antibodies to herpes simplex and cytomegaloviruses [Feorino et al, 1977;Furukawa et al, 1975; Gelb et al, 1981;Keller et al, 19761 are conspicuously absent in tests using VZVinfected cells as substrates.…”

Section: Discussionmentioning

confidence: 87%

“…This phenomenon appears to occur early in the infection cycle, as has been shown using guinea pig cytomegalovirus and other animal herpesviruses [Ishak, 1978, 19821. However, the present study shows that varicella zoster virus is unique among the herpesviruses in failing to induce Fc receptors when cxamined by both immunehemadsorption and immunofluorescence techniques. The use of heat- [Feorino et al, 1977;Furukawa et al, 1975;Gelb et al, 1981;Keller et al, 19761 are conspicuously absent in tests using VZVinfected cells as substrates.…”

Section: Discussionmentioning

confidence: 99%

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Absence of IgG Fc receptors on varicella‐zoster virus‐infected cells

Ishak

Andiman

Tucker

1984

Journal of Medical Virology

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Herpesvirus-infected cells usually express receptors for the Fc portion of immunoglobulin G. Varicella-zoster virus has so far been the sole exception in the family. Both immunehemadsorption and immunofluorescence techniques failed to detect the expression of such receptors. This observation excludes the possibility of false-positive results in serological tests for antibodies to this virus. It is possible that the function of these receptors early in infection is not needed in the subsequent reactivation(s) of the virus. No variation has been shown to occur with different isolates.

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Section: Discussionmentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Absence of IgG Fc receptors on varicella‐zoster virus‐infected cells

Ishak

Andiman

Tucker

1984

Journal of Medical Virology

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“…By contrast, 10to 20-fold-lower concentrations of antibody were sufficient to demonstrate Fc binding in the HSV system (6,7,26). In earlier investigations of the VZV FcR, conditions which were favorable for detection of FcR activity in HSV-infected cells failed to uncover FcR activity in VZV-infected cells (12,14,19). This discrepancy is most likely due to the lower affinity of the VZV receptor for Ig.…”

Section: Discussionmentioning

confidence: 94%

Receptor properties of two varicella-zoster virus glycoproteins, gpI and gpIV, homologous to herpes simplex virus gE and gI

Litwin

Jackson

Grose

1992

J Virol

122

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The varicella-zoster virus (VZV) genome contains 70 reading frames (ORF), 5 of which encode the glycoproteins gpl, gpII, gpIII, gprV, and gpV. ORF 67 and 68 lie adjacent to each other in the unique short region of the VZV genome and code for gpIV and gpl, respectively. These two genes, which are contained within the HindIII C fragment of the VZV genome, were subcloned in the correct orientation downstream from the promoter regions of the eukaryotic expression vectors pCMV5 and pBJ. After transfection, 5 to 20% of the Cos cells bound antibody specific for the given glycoprotein. In this study, it was shown that only the cells transfected with the gpI construct bound to the Fc fragment of human immunoglobulin G. Neither the transfected gpIV gene product nor the vector only bound to the Fc fragment. Thus, VZV gpI is confirmed to be the VZV-encoded Fc-binding glycoprotein. Like the wild-type form of gpI expressed in VZV-infected cells, gpl precipitated from transfected cells contained both N-linked and 0-linked glycans and was heavily sialated. In addition, the transfected gpl gene product was phosphorylated both in cell culture and in protein kinase assays by mammalian casein kinases I and II. Extensive computer-assisted analyses of the VZV gpl sequence, as well as those of alphaherpesviral homolog glycoproteins, disclosed properties similar to those of other cell surface receptors; these included (i) exocytoplasmic regions rich in cysteine residues, (ii) membrane-proximal regions with potential 0-linked glycosylation sites, and (iii) cytoplasmic domains with consensus phosphorylation sites.

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“…HSV gE has been shown to function as a receptor for the Fc component of immunoglobulin molecules (1). There are conflicting reports on whether VZV produces an Fc receptor (17,21,35), and we are aware of no information on whether PRV encodes an Fc receptor. Clearly, PRV gI and VZV gpl would be candidates for Fc receptor molecules in these viruses.…”

Section: Gcgatccggagaaaccggaagtgacgaatgggcccaactatggcgtgaccgccagccgccmentioning

confidence: 98%

Use of lambda gt11 to isolate genes for two pseudorabies virus glycoproteins with homology to herpes simplex virus and varicella-zoster virus glycoproteins

Petrovskis¹,

Timmins²,

Post³

1986

J Virol

108

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A library of pseudorabies virus (PRV) DNA fragments was constructed in the expression cloning vector Agtll. The library was screened with antisera which reacted with mixtures of PRV proteins to isolate recombinant bacteriophages expressing PRV proteins. By the nature of the Agtll vector, the cloned proteins were expressed in Escherichia coli as I-galactosidase fusion proteins. The fusion proteins from 35 of these phages were purified and injected into mice to raise antisera. The antisera were screened by several different assays, including immunoprecipitation of [14C]glucosamine-labeled PRV proteins. This method identified phages expressing three different PRV glycoproteins: the secreted glycoprotein, gX; gI; and a glycoprotein that had not been previously identified, which we designate gp63. The gp63 and gI genes map adjacent to each other in the small unique region of the PRV genome. The DNA sequence was determined for the region of the genome encoding gp63 and gI. It was found that gp63 has a region of homology with a herpes simplex virus type 1 (HSV-1) protein, encoded by US7, and also with varicella-zoster virus (VZV) gpIV. The gI protein sequence has a region of homology with HSV-1 gE and VZV gpl. It is concluded that PRV, HSV, and VZV all have a cluster of homologous glycoprotein genes in the small unique components of their genomes and that the organization of these genes is conserved. * Corresponding author. another major glycoprotein, glil, has been mapped (40) and shown to have homology with the HSV gC gene (39). The gene for a minor PRV glycoprotein, gp5O, was mapped by

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Varicella-Zoster Virus Fails to Induce Immunoglobulin G Fc Receptors in Infected Human Cells

Cited by 7 publications

References 8 publications

Absence of IgG Fc receptors on varicella‐zoster virus‐infected cells

Absence of IgG Fc receptors on varicella‐zoster virus‐infected cells

Receptor properties of two varicella-zoster virus glycoproteins, gpI and gpIV, homologous to herpes simplex virus gE and gI

Use of lambda gt11 to isolate genes for two pseudorabies virus glycoproteins with homology to herpes simplex virus and varicella-zoster virus glycoproteins

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