出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/09/15 21:43:30」(JST)
A slow virus is a virus, or a viruslike agent, etiologically associated with a disease, having a long incubation period of months to years and then a gradual onset of symptoms which progress slowly but irreversibly and terminate in a severe compromised state or, more commonly, death.
A slow virus disease is a disease that, after an extended period of latency, follows a slow, progressive course spanning months to years, frequently involving the central nervous system and ultimately leading to death. Examples include the Visna-Maedi virus, in the genus Lentivirus (family Retroviridae), that causes encephalitis and chronic pneumonitis in sheep, and subacute sclerosing panencephalitis which is apparently caused by the measles virus,[1] as well as Paget's Disease of Bone (Osteitis Deformans) which is associated with paramyxoviridae, especially RSV and Rubeola (Measles).
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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 these slow viruses. This may be in part because the host has acclimated to the virus, or more likely because the host must be immunocompromised in order for many of these slow virus infections to emerge, so the immune system is at a disadvantage from the start.
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| Virus | Virus family | Disease | Typical latency | Transmitted by |
|---|---|---|---|---|
| JC Virus | Polyomavirus | Progressive multifocal leukoencephalopathy | Years to Life§ | Unknown; Contaminated water? |
| BK Virus | Polyomavirus | BK Nephropathy | Years to life§ | Unknown; respiratory spread/urine? |
| Rubeola (Measles) | Paramyxovirus | Subacute Sclerosing Panencephalitis | 1–10 years | Respiratory droplets |
| Rubella | Togaviridae | Progressive Rubella Panencephalitis | 10–20 years | Respiratory droplets |
| HIV | Retrovirus | AIDS | 5–10 years | Infected blood or other body fluids |
| HTLV 1 | Retrovirus | Adult T-cell Leukemia/Lymphoma | 10–30 years | Infected blood or other body fluids |
| HTLV 2 | Retrovirus | Atypical Hairy Cell Leukemia | 10–30 years | Infected blood or other body fluids |
| Rabies Virus | Rhabdoviridae | Rabies | 3–12 weeks | Bite of an infected animal |
Transmissible spongiform encephalopathies (TSEs), including Kuru and Creutzfeldt–Jakob disease of humans, scrapie of sheep, and bovine spongiform encephalopathy (BSE) of cattle, were previously classified as slow virus diseases as well. 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, but they contain no DNA or RNA so they are not viruses.[2] 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[citation needed]
Prions are so named because they appear to contain only protein.[3] 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(GPI)-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.[4]
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.
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 spongeform 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.
The clinical presentation of prion diseases will vary from patient to patient. However, some general characteristics of prion diseases are listed below.
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| リンク元 | 「スローウイルス」「遅発性ウイルス」 |
| 拡張検索 | 「slow virus infection」「slow virus disease」 |
| 関連記事 | 「slow」「slowing」「virus」 |
遅発性ウイルス感染症、スローウイルス感染症、スローウイルス感染