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Varicella-zoster virus-specific gp140: a highly immunogenic and disulfide-linked structural glycoprotein
Abstract:
A 140,000-dalton disulfide-linked glycoprotein (gp140) specified by varicella-zoster virus (VZV) in infected cultured cells was identified and precipitated by two murine monoclonal antibodies (VZ-151 and VZ-158). When analyzed under reducing conditions by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gp140 was cleaved predominantly into a 66,000 lower-molecular-weight product (gp66). This protein was classified as a viral structural component, since it was observed in the polypeptide profile of metrizamide gradient-purified enveloped virions. By immunofluorescence analyses with a monoclonal antibody probe, gp140 expression was documented to be highly conserved both within cultured cells inoculated with homologous (VZV-Oka) and heterologous (VZV-32) strains and in infected human tissues from chicken pox and zoster patients. That the glycoprotein was highly immunogenic was confirmed by the presence of high-titer anti-gp140 antibody in the sera of both hyperimmunized laboratory animals and naturally infected humans. Temporally, the humoral response to gp140 following primary VZV infection preceded that against the other viral glycoproteins. These studies describe, therefore, an immunogenic, disulfide-linked viral structural glycoprotein, which must be included among the other five previously described VZV-specific fucosylated species--gp118, gp98, gp62, and gp45.
Insights
Researchers identified a new varicella-zoster virus (VZV) glycoprotein, gp140. This immunogenic viral structural component is conserved across VZV strains and is an early target of the human immune response.
Area of Science:
- Virology
- Immunology
- Molecular Biology
Background:
- Varicella-zoster virus (VZV) causes chickenpox and shingles.
- Understanding VZV structural proteins is crucial for vaccine development and antiviral strategies.
- Previous studies identified several VZV-specific fucosylated glycoproteins.
Purpose of the Study:
- To identify and characterize a novel disulfide-linked glycoprotein (gp140) of VZV.
- To determine the structural properties and viral localization of gp140.
- To assess the immunogenicity and temporal expression of gp140 during VZV infection.
Main Methods:
- Identification and precipitation of gp140 using monoclonal antibodies (VZ-151, VZ-158).
- Analysis of gp140 cleavage products under reducing conditions using SDS-PAGE.
- Detection of gp140 in purified VZV virions and infected cells/tissues via immunofluorescence and Western blotting.
Main Results:
- A 140,000-dalton disulfide-linked glycoprotein (gp140) specified by VZV was identified.
- gp140 is cleaved into a 66,000-dalton product (gp66) under reducing conditions and is a viral structural component.
- gp140 expression is conserved across VZV strains and in infected human tissues; it is highly immunogenic and elicits an early humoral response.
Conclusions:
- gp140 is an immunogenic, disulfide-linked VZV structural glycoprotein.
- gp140 should be considered among the previously described VZV-specific fucosylated glycoproteins.
- The early immunogenicity of gp140 suggests its potential role in VZV pathogenesis and immune evasion.