Book chapter
Structure-Function Profiles of Nine Varicella-zoster Virus Glycoproteins: Endocytosis, Entry and Egress
Alphaherpesviruses: Molecular Virology, pp.153-174
Caister Academic Press
01/01/2011
Abstract
Varicella zoster virus has a smaller genome than herpes simplex virus and therefore encodes fewer glycoproteins. In this chapter, nine VZV glycoproteins are profiled, including gE, gI, gC, gH, gL, gB, gK, gM, and gN. Although all VZV glycoproteins have HSV homologues, functions occasionally have greatly shifted. For example, VZV gE is the predominant VZV glycoprotein and exists as a monomer, dimer and trimer, as well as a gE/gI complex. VZV gE is essential, unlike HSV gE. Even though essential, mutations in gE had been detected in wild type VZV strains that exhibit an accelerated cell-spread phenotype. The VZV gC glycoprotein differs from HSV gC in that both transcription and translation of VZV gC are remarkably delayed in cultured cells; often VZV gC protein is difficult to detect altogether. The VZV gH/gL complex resembles the HSV gH/gL complex is that both are critical for virus induced fusion. Fusion is a prominent feature of VZV infected cells. Neutralization antibody to VZV gH dramatically reduces the spread of virus and limits pathogenesis in the skin. The VZV gB glycoprotein is also involved in virus-induced fusion. Of interest, four VZV glycoproteins (gE, gI, gH and gB) have functional endocytosis motifs in their cytoplasmic tail. Thus, all four are internalized from the cell surface in clathrin coated vesicles. This pathway appears critical for the process of virion envelopment in the assembly compartment. Even though abundant amounts of most glycoproteins are produced in cell culture, assembly of fully enveloped and infectious VZV particles rarely occurs. The particle plaque forming unit ratio remains an extremely high 40,000:1. Likewise, the aberrant assembly process severely limits any assessment of egress mechanisms.
Details
- Title: Subtitle
- Structure-Function Profiles of Nine Varicella-zoster Virus Glycoproteins: Endocytosis, Entry and Egress
- Creators
- Charles Grose - Univ Iowa, Childrens Hosp, Iowa City, IA 52242 USASusan Vleck - Stanford UniversityOdd Andre Karlsen - University of BergenEduardo A. Montalvo
- Contributors
- S K Weller (Editor)
- Resource Type
- Book chapter
- Publication Details
- Alphaherpesviruses: Molecular Virology, pp.153-174
- Publisher
- Caister Academic Press; WYMONDHAM
- Number of pages
- 22
- Language
- English
- Date published
- 01/01/2011
- Academic Unit
- Stead Family Department of Pediatrics; Infectious Disease (Pediatrics)
- Record Identifier
- 9984354403302771
Metrics
10 Record Views