A collaboration solves the herpes virus protein structure providing new drug therapy directions

The genome structure of a herpesvirus isolated from primary cultures of kidney cells from the cottontail rabbit Sylvilagus floridanus was elucidated by using electron microscopy and restriction enzyme analysis. The map is at the same magnification and is contoured at the same level as the KSHV capsid shown in Fig. All members of the herpesviridae contain within their large tegument protein a cysteine protease module that displays deubiquitinating activity. DNA binding and transcriptional activation domains were found in the IE protein. We demonstrate that ORF112 also binds CpG repeats in the left-handed conformation, and moreover, its structure at 1.75 Å reveals the Zalpha fold found in ADAR1, DAI, PKZ, and E3L. Both peptides are shown to bind the CXC chemokine receptor 4 (CXCR4). In this study, researchers determined the structure of this key protein complex and realized it did not resemble the structure of other known fusogens.

There is no cure for herpes viruses. Upon infection, the viruses remain in the body for life and can stay inactive for long periods of time. When active, however, different herpes viruses can cause cold sores, blindness, encephalitis or cancers. Use which would be defamatory, pornographic or otherwise unlawful is prohibited. In immunogold electron microscopy (EM) experiments, they observed that an anti-UL6 antibody labeled one vertex site per capsid. Each of these regions are bracketed by terminal repeats. HVEM is known for its ability to provide costimulatory signals to T cells in response to the TNF-related cytokine LIGHT (5, 6).

Whereas most other enveloped viruses use a single viral catalyst called a fusogen, herpes viruses inexplicably require two conserved fusion-machinery components, gB and the heterodimer gH-gL, plus other nonconserved components. gB is a class III viral fusogen, but, unlike other members of its class, it does not function alone.