Project Details
Description
All Herpes viruses possess a proteinaceous layer termed tegument which lines the inner surface
of their envelope. Tegument is acquired both at the inner nuclear membrane during primary
envelopment, and in the cytoplasm during secondary envelopment. These tegument layers are
morphologically distinct, however, little is known of how their molecular compositions differ.
Furthermore, the mechanisms by which tegument proteins become bound to membranes and
incorporated into the assembling HSV particle are poorly understood.
We have identified a 42 amino acid membrane targeting motif in the amino terminus of vhs, a
tegument component that is an important neurovirulence determinant. This membrane sorting motif is
also sufficient to direct a GFP reporter into the HSV particle. Furthermore, we have shown that vhs
binds to the cytoplasmic tail of the envelope glycoprotein gH. The aims of this proposal dissect the
molecular details of membrane targeting by the amino terminus of vhs, tests the role of gH in this
process and examines the nature of vhs in the perinuclear HSV particle. We also use newly
developed methodologies to investigate the general composition and function of the perinuclear HSV
particle, examine targeting of vhs to the perinuclear virion and compare the envelope and tegument of
these poorly characterized particles with those of mature virions.
Status | Finished |
---|---|
Effective start/end date | 9/15/08 → 8/31/10 |
ASJC
- Structural Biology
- Medicine(all)
- Immunology and Microbiology(all)
- Spectroscopy
Fingerprint
Explore the research topics touched on by this project. These labels are generated based on the underlying awards/grants. Together they form a unique fingerprint.