Every infectious agent is different, but in general, slow viruses: Additionally, the immune system seems to plays a limited role, or no role, in protection from many of these slow viruses. This may be due to the slow replication rates some of these agents exhibit, preexisting immunosuppression, or, in the case of prions, the identity of the agent involved.
Some examples of viral agents
Prions: "atypical slow viruses"
, including kuru and Creutzfeldt–Jakob disease of humans, scrapie of sheep, and bovine spongiform encephalopathy of cattle, were previously classified as slow virus diseases. However, TSEs are more correctly classified as prion diseases. Prions are misfolded proteins that are "infectious" because they can induce misfolding in other previously normal proteins; however, they do not contain DNA or RNA so they cannot be classified as viruses. Before scientists knew the cause of spongiform encephalopathies, they hypothesized that small virus particles, which they termed virions, were to blame. Once it was discovered that prions were the real cause of TSEs and that prions contained no nucleic acid, the term virions was discarded and these particles were renamed prions. A minority of researchers still believe, however, that prion diseases are caused by an as-yet unidentified slow virus, although there is little evidence to support this finding, as Ma and colleagues have created a recombinant prion protein. Prions are so named because they appear to contain only protein. No evidence of nucleic acid has been found in any prion particle studied. Treatments that destroy protein, like denaturation, destroy prion infectivity, but treatments that destroy nucleic acids, like UV radiation, do not destroy prion infectivity. The prion protein is known as PrP and is a cell surface glycophosphatidylinositol-anchored protein. Its normal function in the body is unknown, though presumably it serves, or served, some purpose because it is coded for by a host gene. The infectious form of PrP has the same amino acid sequence and the same post-translational modifications as the normal form, but it has a different tertiary conformation. The normal PrP contains many alpha-helices, whereas the disease-associated form contains many beta-pleated sheets. It is this conformational change from mostly alpha-helices to mostly beta-pleated sheets that gives the prion its infectious ability. The disease-associated form of the prion protein is commonly referred to as PrPsc because it was first found in scrapie infections in sheep. The diseased form is also occasionally called PrPres because it is more resistant to protease than the normal, non-disease associated form.
Cause
In some cases, the cause of prion diseases is known. Ingestion of a copy of an abnormally folded, infectious PrP can induce a spongiform encephalopathy in the consumer. For example, kuru is passed through the ritual consumption of brain material in some tribal cultures, and bovine spongiform encephalopathy is thought to have developed from the use of prion-infected sheep protein in cattle feed. However, some cases of spongiform encephalopathies appear to be sporadic, and it is not known in these cases what causes the first prion protein to change its conformation and become infectious. Once one abnormal prion protein exists, however, it can induce the conformational change from predominantly α-helix to predominately β-pleated sheet in neighboring proteins.
Disease presentation
The clinical presentation of prion diseases will vary from patient to patient. However, some general characteristics of prion diseases are listed below.
