Journal article
Assembly and processing of the disulfide-linked varicella-zoster virus glycoprotein gpII(140)
Journal of virology, Vol.61(9), pp.2877-2884
09/1987
DOI: 10.1128/JVI.61.9.2877-2884.1987
PMCID: PMC255809
PMID: 3039175
Abstract
Varicella-zoster virus (VZV) specifies the synthesis of at least four families of glycoproteins, which have been designated gpI, gpII, gpIII, and gpIV. In this report we describe the assembly and processing of VZV gpII, a structural protein of an apparent Mr of 140,000, which is the homolog of gB of herpes simplex virus. For these studies, we used two anti-gpII monoclonal antibodies which exhibited both complement-independent neutralization activity and inhibition of virus-induced cell-to-cell fusion. Pulse-chase labeling experiments identified a 124,000-Mr intermediate which was chased to the mature 140,000-Mr product when analyzed in nonreducing gels; in the presence of a reducing agent, the native gp140 was cleaved into two closely migrating species (gp66 and gp68). The biosynthesis of VZV gpII was further analyzed in the presence of the following inhibitors of glycoprotein processing: tunicamycin, monensin, castanospermine, swainsonine, and deoxymannojirimycin. All intermediate and mature forms were digested with endoglycosidases H and F, neuraminidase, and O-glycanase to further define high-mannose, complex, and O-linked glycans. Finally, the addition of sulfate residues was investigated. This characterization of VZV gpII revealed the following results. (i) gp128 and gp124 were early high-mannose forms, (ii) gp126 was an intermediate form with complex N-linked oligosaccharides, (iii) gp130 was a later intermediate with both N-linked and O-linked glycans, and (iv) the mature product gp140 contained a mixture of N-linked and O-linked glycans which were both sialated and sulfated. Further investigations indicated that gpII sulfation was inhibited by tunicamycin and castanospermine but not by deoxymannojirimycin or swainsonine. We also concluded that VZV gpII displayed many biological and biochemical properties similar to those of its herpes simplex virus homolog gB.
Details
- Title: Subtitle
- Assembly and processing of the disulfide-linked varicella-zoster virus glycoprotein gpII(140)
- Creators
- E A MontalvoC Grose
- Resource Type
- Journal article
- Publication Details
- Journal of virology, Vol.61(9), pp.2877-2884
- DOI
- 10.1128/JVI.61.9.2877-2884.1987
- PMID
- 3039175
- PMCID
- PMC255809
- ISSN
- 0022-538X
- eISSN
- 1098-5514
- Grant note
- AI 22795 / NIAID NIH HHS
- Language
- English
- Date published
- 09/1987
- Academic Unit
- Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
- Record Identifier
- 9984093488702771
Metrics
22 Record Views