Herpes Tips

Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosi

Antiviral drugs are a class of medication used specifically for treating viral infections.[1] Like antibiotics and broad-spectrum antibiotics for bacteria, most antivirals are used for specific viral infections, while a broad-spectrum antiviral is effective against a wide range of viruses.[2] Unlike most antibiotics, antiviral drugs do not destroy their target pathogen; instead they inhibit their development. To gain a better understanding of the tegumentation process, we initiated studies that focused on the herpes simplex virus type 1 (HSV-1) tegument protein pUL46. Further studies show that HIV uses cytoplasmic dynein and the microtubule network to migrate toward the nucleus. We propose that the incoming capsids bind to microtubules and use dynein to propel them from the cell periphery to the nucleus. To gain insight into the mechanism of defensin-mediated neutralization, we analyzed the specificity of the AdV-defensin interaction. Conversely, the levels of activated Ras and mitogen-activated protein kinase (MAPK), and the expression and stabilization of the transcription factor c-Fos were significantly increased in cells infected with HSV-2 or a revertant virus [HSV-2(R)] but not with ICP10ΔPK. The DNA was released within 30 min after a shift to the permissive temperature.

Moreover, the amino-terminal one-third of the UL25 protein is particularly important in DNA binding and forms a homo-oligomer. To study the fate of UL25 at very early stages of infection, immunofluorescence experiments were performed on invading PrV particles in the presence or absence of drugs that specifically depolymerize components of the cytoskeleton. W. Newcomb, J. Exposure on the surface is consistent with the view that UL25 is added to the capsid as DNA is packaged or during late stages of the packaging process. The viral genome is inserted into a preformed protein shell known as the procapsid, where it assumes a highly compact, ordered state with liquid crystalline density (2).