Prion, an abnormal form of a normally harmless protein found in

the brain that is responsible for a variety of fatal neurodegenerative

diseases of animalIn the early 1980s American neurologist Stanley B.
Prusiner anPrions are unlike all other known disease-causing agents in that
they appear to lack nucleic acid—i.e., DNA or RNA—which is the genetic
material that all other organisms contain. Another unusual characteristic of
prions is that they can cause hereditary, infectious, and sporadic forms of
disease—for example, Creutzfeldt-Jakob diseased colleagues identified the
“proteinaceousViroid, an infectious particle smaller than any of the known
viruses, an agent of certain plant diseases. The particle consists only of an
extremely small circular RNA (ribonucleic acid) molecule, lacking
the protein coat of

Viroid

Scientific classification

(unranked): Subviral agents

(unranked): Viroid

Families

Pospiviroidae
Avsunviroidae

Viroids are the smallest infectious pathogens

known. They are composed solely of a short
strand of circular, single-stranded RNA without
protein coat. All known viroids are inhabitants of
higher plants, in which most cause diseases, some
of which are of slight to catastrophic economic
importance.
The first recognized viroid, the pathogenic agent of
the potato spindle tuber disease, was discovered,
initially molecularly characterized, and named
by Theodor Otto Diener, plant pathologist at the
U.S Department of Agriculture's Research Center
in Beltsville, Maryland, in 1971.[1][2] This viroid is
now called Potato spindle tuber viroid, abbreviated
PSTVd
a virus infectious particle A protein as a stand-
alone infectious agent stands in contrast to all other known infectious agents such as
viruses, bacteria, fungi, and parasites, all of which contain nucleic acids (DNA, RNA, or both).
For this reason, a minority of researchers still consider the prion/TSE hypothesis unproven.[7] The
protein that prions are made of (PrP) is found throughout the body, even in healthy people and
animals. However, PrP found in infectious material has a different structure and is resistant
to proteases, the enzymes in the body that can normally break down proteins. The normal form
of the protein is called PrPC, while the infectious form is called PrPSc — the C refers to 'cellular'

PrP, while the Sc refers to 'scrapie', the prototypic prion disease, occurring in sheep.
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