lordhugo:


Prions are non-living. Like your senses!

Fool, prions/viruses are living things but they only undergo metabolism intra-cellularly in their hosts.
They are obligate parasites.

I guess you failed medical virology in school.

TheSonOfMark:

Fool, prions/viruses are living things but they only undergo metabolism intra-cellularly in their hosts.
They are obligate parasites.

I guess you failed medical virology in school.

A prion (Listeni/ˈpriːɒn/[1]) is a protein that can fold in multiple, structurally distinct ways, at least one of which is transmissible to other prion proteins. It is this form of replication that leads to disease that is similar to viral infection. The word prion, coined in 1982 by Stanley B. Prusiner, is derived from the words protein and infection, in reference to a prion's ability to self-propagate and transmit its conformation to other prions.[2] While several yeast proteins have been identified as having prionogenic properties, the first prion protein was discovered in mammals and is referred to as the major prion protein (PrP). This infectious agent causes mammalian transmissible spongiform encephalopathies, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease" and scrapie in sheep. In humans, PrP causes Creutzfeldt-Jakob Disease (CJD), variant Creutzfeldt-Jakob Disease (vCJD), Gerstmann–Sträussler–Scheinker syndrome, Fatal Familial Insomnia and kuru.[3]

A protein as an infectious agent stands in contrast to all other known infectious agents, like viruses, bacteria, fungi, or parasites—all of which must contain nucleic acids (either DNA, RNA, or both). All known prion diseases in mammals affect the structure of the brain or other neural tissue and all are currently untreatable and universally fatal.[4]

While PrP is considered the only mammalian prion, prion-like domains have been found in a variety of other mammalian proteins. Some of these proteins have been implicated in the ontogeny of age-related degenerative disorders such as amyotrophic lateral sclerosis (ALS), frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U), Alzheimer's disease, and Huntington's disease.[5] This has given rise to the 'prion paradigm', where otherwise harmless proteins can be converted to a pathogenic form by a small number of misfolded, nucleating proteins.[6]

Prions are not considered living organisms because they are misfolded protein molecules which may propagate by transmitting a misfolded protein state. If a prion enters a healthy organism, it induces existing, properly folded proteins to convert into the misfolded prion form. In this way, the prion acts as a template to guide the misfolding of more proteins into prion form. In yeast, this refolding is assisted by chaperone proteins such as Hsp104p. These refolded prions can then go on to convert more proteins themselves, leading to a chain reaction resulting in large amounts of the prion form.[7] All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. Amyloid aggregates are fibrils, growing at their ends, and replicating when breakage causes two growing ends to become four growing ends. The incubation period of prion diseases is determined by the exponential growth rate associated with prion replication, which is a balance between the linear growth and the breakage of aggregates.[8] (Note that the propagation of the prion depends on the presence of normally folded protein in which the prion can induce misfolding; animals that do not express the normal form of the prion protein can neither develop nor transmit the disease.)

Prion aggregates are extremely stable and accumulate in infected tissue, causing tissue damage and cell death.[9] This structural stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult. Prion structure varies slightly between species, but nonetheless prion replication is subject to occasional epimutation and natural selection just like other forms of replication.[10]

All known mammalian prion diseases are caused by the so-called prion protein, PrP. The endogenous, properly folded form is denoted PrPC (for Common or Cellular), whereas the disease-linked, misfolded form is denoted PrPSc (for Scrapie, after one of the diseases first linked to prions and neurodegeneration.)[11][12] The precise structure of the prion is not known, though they can be formed by combining PrPC, polyadenylic acid, and lipids in a Protein Misfolding Cyclic Amplification (PMCA) reaction.[13] Proteins showing prion-type behavior are also found in some fungi, which has been useful in helping to understand mammalian prions. Fungal prions do not appear to cause disease in their hosts.[14]

Braintouch:
Super boring. . .

KingTom:

That means Akwa Ibom is beautiful You feel say I be Fee Dee Fee like you wey no dey pan national

lordhugo:


Trying to argue with someone who is full of himself is even more draining.

How r you today?

lordhugo:




https://en.wikipedia.org/wiki/Prion

Somewhere out there is a tree, tirelessly producing oxygen so you can breathe. I think you owe it an apology

LordHugo, is a parasite a living organism? Yes, right? A virus is also a parasite, right? Why then did you opine that viruses are non-living?

Obviously did I am a biomedical student, did you? Mediocre!

TheSonOfMark:

LordHugo, is a parasite a living organism? Yes, right? A virus is also a parasite, right? Why then did you opine that viruses are non-living?


Viruses/prions are capsule-sheated organisms with nucleic acid (the folded protein) which are obligate i.e depend on their hosts. VIRUSES REPLICATE IN HOST CELLS. ONLY LIVING THINGS REPLICATE.


Obviously you didn't know I am a biomedical student, did you? Mediocre!

lordhugo:


I said prions! I have never mentioned viruses.

Prions are unique pathogens in that they appear to have no nucleic acid and thereby differ from viruses, bacteria, fungi and other pathogens. Prions are resistant to procedures that break down nucleic acid and destroy biological forms of pathogens.

I am a geologist and i wonder why i can make this differentiation and you can't. (Being a Bio-medical such and shi.t)

If we doubled your IQ score it would still be negative!

Foòl, prions are the progenitors of viruses just like archae developed into bacteria.

The prions are not just folded protein (nucleid acid), they are more.

Prions are the parasites for encephalopathy. Only living things are pathogenic.

You really are a fool. Visit reknowned medical websites and stop gulping the gibberish on Wikipedia.

TheSonOfMark:

Foòl, prions are the progenitors of viruses just like archae developed into bacteria.

The prions are not just folded protein (nucleid acid), they are more.

Prions are the parasites for encephalopathy. Only living things are pathogenic.

You really are a fool. Visit reknowned medical websites and stop gulping the gibberish on Wikipedia.

TheSonOfMark:

Foòl, prions are the progenitors of viruses just like archae developed into bacteria.
The prions are not just folded protein (nucleid acid), they are more.
Prions are the parasites for encephalopathy. Only living things are pathogenic.
You really are a fool. Visit reknowned medical websites and stop gulping the gibberish on Wikipedia.

TheSonOfMark:

LordHugo the rètard, are you reading?
Are you now realizing that prions are parasites and all parasites are living organisms?
I am here to tutor you ignorant nitwits.

TheSonOfMark:
LORDHUGO, VISIT THIS WEBSITE TO CLEAR YOUR DOUBT: http://ghr.nlm.nih.gov/condition/prion-disease

What is prion disease?
Prion disease represents a group of conditions that affect the nervous system in humans and animals. In people, these conditions impair brain function, causing changes in memory, personality, and behavior; a decline in intellectual function (dementia); and abnormal movements, particularly difficulty with coordinating movements (ataxia). The signs and symptoms of prion disease typically begin in adulthood and worsen with time, leading to death within a few months to several years.
How common is prion disease?
These disorders are very rare. Although the exact prevalence of prion disease is unknown, studies suggest that this group of conditions affects about one person per million worldwide each year. Approximately 350 new cases are reported annually in the United States.
What genes are related to prion disease?
Between 10 and 15 percent of all cases of prion disease are caused by mutations in the PRNP gene. Because they can run in families, these forms of prion disease are classified as familial. Familial prion diseases, which have overlapping signs and symptoms, include familial Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome (GSS), and fatal familial insomnia (FFI).
The PRNP gene provides instructions for making a protein called prion protein (PrP). Although the precise function of this protein is unknown, researchers have proposed roles in several important processes. These include the transport of copper into cells, protection of brain cells (neurons) from injury (neuroprotection), and communication between neurons. In familial forms of prion disease, PRNP gene mutations result in the production of an abnormally shaped protein, known as PrPSc, from one copy of the gene. In a process that is not fully understood, PrPSc can attach (bind) to the normal protein (PrPC) and promote its transformation into PrPSc. The abnormal protein builds up in the brain, forming clumps that damage or destroy neurons. The loss of these cells creates microscopic sponge-like holes (vacuoles) in the brain, which leads to the signs and symptoms of prion disease.
The other 85 to 90 percent of cases of prion disease are classified as either sporadic or acquired. People with sporadic prion disease have no family history of the disease and no identified mutation in the PRNP gene. Sporadic disease occurs when PrPC spontaneously, and for unknown reasons, is transformed into PrPSc. Sporadic forms of prion disease include sporadic Creutzfeldt-Jakob disease (sCJD), sporadic fatal insomnia (sFI), and variably protease-sensitive prionopathy (VPSPr).
Acquired prion disease results from exposure to PrPSc from an outside source. For example, variant Creutzfeldt-Jakob disease (vCJD) is a type of acquired prion disease in humans that results from eating beef products containing PrPSc from cattle with prion disease. In cows, this form of the disease is known as bovine spongiform encephalopathy (BSE) or, more commonly, "mad cow disease." Another example of an acquired human prion disease is kuru, which was identified in the South Fore population in Papua New Guinea. The disorder was transmitted when individuals ate affected human tissue during cannibalistic funeral rituals.
Rarely, prion disease can be transmitted by accidental exposure to PrPSc-contaminated tissues during a medical procedure. This type of prion disease, which accounts for 1 to 2 percent of all cases, is classified as iatrogenic.
Read more about the PRNP gene.
How do people inherit prion disease?
Familial forms of prion disease are inherited in an autosomal dominant pattern, which means one copy of the altered PRNP gene in each cell is sufficient to cause the disorder. In most cases, an affected person inherits the altered gene from one affected parent. In some people, familial forms of prion disease are caused by a new mutation in the gene that occurs during the formation of a parent's reproductive cells (eggs or sperm) or in early embryonic development. Although such people do not have an affected parent, they can pass the genetic change to their children.
The sporadic, acquired, and iatrogenic forms of prion disease, including kuru and variant Creutzfeldt-Jakob disease, are not inherited.
Where can I find information about diagnosis or management of prion disease?
These resources address the diagnosis or management of prion disease and may include treatment providers.
Creutzfeldt-Jakob Disease Foundation: Suggestions for Patient CareThis link leads to a site outside Genetics Home Reference.
Gene Review: Genetic Prion DiseasesThis link leads to a site outside Genetics Home Reference.
Genetic Testing Registry: Genetic prion diseasesThis link leads to a site outside Genetics Home Reference.
MedlinePlus Encyclopedia: Creutzfeldt-Jakob diseaseThis link leads to a site outside Genetics Home Reference.
MedlinePlus Encyclopedia: KuruThis link leads to a site outside Genetics Home Reference.
University of California, San Fransisco Memory and Aging Center: Living With Creutzfeldt-Jakob DiseaseThis link leads to a site outside Genetics Home Reference.
University of California, San Fransisco Memory and Aging Center: Treatments for Creutzfeldt-Jakob DiseaseThis link leads to a site outside Genetics Home Reference.
You might also find information on the diagnosis or management of prion disease in Educational resources and Patient support.
General information about the diagnosis and management of genetic conditions is available in the Handbook. Read more about genetic testing, particularly the difference between clinical tests and research tests.
To locate a healthcare provider, see How can I find a genetics professional in my area? in the Handbook.
Where can I find additional information about prion disease?
You may find the following resources about prion disease helpful. These materials are written for the general public.
MedlinePlus - Health information (5 links)
Genetic and Rare Diseases Information Center - Information about genetic conditions and rare diseases (3 links)
Additional NIH Resources - National Institutes of Health (5 links)
Educational resources - Information pages (11 links)
Patient support - For patients and families (6 links)
You may also be interested in these resources, which are designed for healthcare professionals and researchers.
Gene ReviewsThis link leads to a site outside Genetics Home Reference. - Clinical summary
Genetic Testing Registry - Repository of genetic test information (5 links)
ClinicalTrials.govThis link leads to a site outside Genetics Home Reference. - Linking patients to medical research
PubMedThis link leads to a site outside Genetics Home Reference. - Recent literature
OMIM - Genetic disorder catalog (4 links)
What other names do people use for prion disease?
inherited human transmissible spongiform encephalopathies
prion-associated disorders
prion-induced disorders
prion protein diseases
transmissible dementias
transmissible spongiform encephalopathies
TSEs
For more information about naming genetic conditions, see the Genetics Home Reference Condition Naming Guidelines and How are genetic conditions and genes named? in the Handbook.
What if I still have specific questions about prion disease?
Ask the Genetic and Rare Diseases Information CenterThis link leads to a site outside Genetics Home Reference..
Where can I find general information about genetic conditions?
The Handbook provides basic information about genetics in clear language.
What does it mean if a disorder seems to run in my family?
What are the different ways in which a genetic condition can be inherited?
If a genetic disorder runs in my family, what are the chances that my children will have the condition?
Why are some genetic conditions more common in particular ethnic groups?
These links provide additional genetics resources that may be useful.
Genetics and Health
Resources for Patients and Families
Resources for Health Professionals
What glossary definitions help with understanding prion disease?
ataxia ; autosomal ; autosomal dominant ; cell ; dementia ; embryonic ; encephalopathy ; familial ; family history ; gene ; iatrogenic ; inherited ; injury ; insomnia ; mutation ; nervous system ; new mutation ; population ; prevalence ; prion ; protease ; protein ; reproductive cells ; sperm ; sporadic ; syndrome ; tissue ; transformation

ronald4lif:


Who is he?. Does he have an alternate account

Are you the one?

AgapeCharis:
Are you the one?

Tashaamania:
Agapecharis, what's MrCork's other moniker?

Don't tell me to mind my business pls

His other moniker is MYOB. It's kind of a coincidence cos MYOB means mind your own business.

lordhugo:



[size=20pt]
Prions are Prions!

Viruses are Viruses!

Parasites are Parasites!


Each man to his own !

ALL UNDER GERMS!!!! [/size]

http://www.antimicrobialtestlaboratories.com/bacteria_viruses_fungi_and_parasites.htm

Are you from Dumbfukistan?

You fell out of the stupid tree and hit every branch on the way down.

Interesting.

You remember MR NIGER D in high school, right? REPLICATION is also one of the characteristics of living things, right?
It means ONLY LIVING THINGS REPLICATE.

Answer these:

1. What are prions?

2. Do prions replicate or not?

3. How do organisms commandeer the functionality of a cell?

4. Why do prions secrete enzymes which induce immunologic responses since according to you they are " non-living things"?

If you do not answer these questions you are a mad man.

AgapeCharis:
His other moniker is MYOB. It's kind of a coincidence cos MYOB means mind your own business.

ronald4lif:

You dey squeeze face for ya elder abi?

Tashaamania:

Ronald4lif, help me

Hahahahahahaha
Ronald4lif to help you with what?

Tashaamania:

Ronald4 lif, help me

Nneoma, I've no clue who they are talking about and the mischief maker AgapeCharis is not to be trusted. I take whatever he says with a pinch of salt. In fact, if he tells me good morning I do check my clock to make sure it correspond with what he says.

Kedu ka idi?.

AgapeCharis:
Hahahahahahaha
Ronald4lif to help you with what?

AgapeCharis:
You dey squeeze face for ya elder abi?

ronald4lif:


Nneoma, I've no clue who they are talking about and the mischief maker AgapeC haris is not to be trusted. I take whatever he says with a pinch of salt. In fact, if he tells me good morning I do check my clock to make sure it correspond with what he says.

Kedu ka idi?.

Since when you start dey call Tasha nneoma?

You go let me do something now.

ronald4lif:


Nneoma, I've no clue who they are talking about and the mischief maker AgapeCharis is not to be trusted. I take whatever he says with a pinch of salt. In fact, if he tells me good morning I do check my clock to make sure it correspond with what he says.

Kedu ka idi?.