Prion

Prion
Presented By - Ms Anushka Srivastava

Roll No. - 2081120
Teacher’s Name - Mr Sandeep Saini
Declaration
I hereby declare the project work entitled
“ To study the selected protein which is PRION
and it’s primary, secondary, tertiary and
quaternary structure” submitted to the
department of biochemistry,S.D College,is
prepared by me.
Anushka Srivastava
2081120
1st year Bioinfo (Hons)
● Prion Protein
● Structure hierarchy of Prion protein
The Contents
● Three dimensional representation of prion
protein.
● Prion the infectious Agent
● Prion Diseases
● History Of Prions
● Reference
General Introduction of Prion
Protein Prion Expressed in E.Coli

Prions are misfolded proteins with the ability to transmit their
misfolded shape onto normal variants of the same protein. They
characterize several fatal and transmissible neurodegenerative
diseases in humans and many other animals. It is not known what
causes the normal protein to misfold, but the abnormal
three-dimensional structure is suspected of conferring infectious
properties, collapsing nearby protein molecules into the same
shape. The word prion derives from "proteinaceous infectious
particle".
“Prion' is a term ﬁrst used to describe the
mysterious infectious agent responsible for
several neurodegenerative diseases found in
mammals, including Creutzfeldt-Jakob
disease (CJD) in humans. The word itself
derives from 'proteinaceous infectious
particle'; it refers to the initially heretical
hypothesis that the infectious agent causing
those diseases consists only of protein, with
no nucleic acid genome.”
Structure hierarchy of Prion
protein
Microscopic image of Prion in C.J.D
● Before we dive into prions, it’s necessary to understand the structure of a protein and
how it relates to its function. Proteins actually have 4 levels of structure!
● Proteins are made from strings of amino acids, and these chains (also known as
polypeptides) form their primary structure.
● Depending on these amino acids and the interaction via hydrogen bonding between
them, two types of secondary structures can be formed, namely alpha-helix and
beta-sheets. These structures then fold into three-dimensional structures.
● The folding is driven by hydrophobic interactions. The structure is kept intact via salt
bridges (combinations of hydrogen bonds and ionic bonds) and disulfide bonds. Finally,
multiple subunits come together and form a quaternary structure. This structure acts as
a single unit and performs various functions.
● This means that amino acid sequences determine the structure of the functional
protein.
Next is the connection between structure and
function! Proteins do not randomly bind to their
targets.
They have a speciﬁc active site that is used to bind

and continue its work. So, in the end, if the structure
changes, it would change the shape of the active site.
This would stop the protein from being able to do its

job! Also, in certain cases, a change in structure
would change the function and cause problems, as it
might bind to targets not intended for that particular
protein!
Preview
The prion protein can

exist in multiple isoforms,
predominantly the
cellular, non-infectious
PrPC and the
disease-causing PrPSc.
The prion protein is most
highly expressed in the
central nervous system
(CNS), but it can be found
in other tissues and cell
types as well.
Prion proteins (PrP) found in our body and those that cause diseases are structurally different.
Some of them are even resistant to proteases (enzymes that degrade protein). We will look at
both isoforms.
■ PrPC – These proteins are found on the membranes of cells. They are believed to
play important roles in intracellular signaling and cell adhesion. However, research
is ongoing as the issues related to its function haven’t been solved.
■ PrPSc – This disease-causing prion is protease-resistant. It changes the PrPC by
affecting its conformation. The change in structure changes how it interacts and
interconnects with proteins! The 3-D structure of these prions is not known, but what
we do know is that they have more beta-sheets than the usual alpha-helix structure.
This prion also forms highly structured amyloid fibers. The end of the fiber acts as a
template for other free proteins to attach. Only similar prions with similar amino
acids can bind! Cross-species binding is very rare, but it is possible.
Three dimensional representation of
prion protein.
Microscopic Protein
Prion The Infectious Agent
Infectious Protein
● Some prion disease appear to be infectious.
● That is, one can isolate something from an infected individual, give it to
another individual and that individual will get the disease and make more
of the infectious material.
● This is the behavior one expects for an infectious agent, such as a virus
or bacterium.
Prion Diseases
Microscopic View of a Disease Causing Protein

● As diseases, prion diseases are quite rare and difficult to transmit. But they are also quite scary, because
they are progressive neurodegenerative diseases, with no cure or treatment. They also have the mystique
of being strange, due to the poor understanding of what prions are and how they work.
● The prion disease most in the news is BSE (bovine spongiform encephalopathy), often called mad-cow
disease. It is rather likely that the BSE agent can be transmitted to humans, and cause vCJD (variant
Creutzfeldt-Jakob disease). The number of known vCJD cases in humans is under 200, but there are so
many unknowns, including a possible incubation period of many many years, that this mysterious disease
strikes fear -- at least much uncertainty.
● As we learn more about prion diseases, a new part of the story is emerging. It is possible that a number of
neurodegenerative diseases long considered quite distinct may share some underlying features. These
include Alzheimer's disease, Parkinson's disease, Huntington disease, and the prion diseases. The common
thread may be that all involve misfolded proteins. The reason for the misfolding and the details of the
disease development vary, and there is no implication here that all of these are infectious. In fact, not all
prion diseases are infectious.
Sheep
● Scrapie is the "classic" prion disease and the subject of most early work on this type of disease.
Sheep are not very good lab animals, so progress was slow. Scrapie has been adapted to small lab
animals, including mice and hamsters; much lab work is done with mouse scrapie or hamster scrapie.
Cattle
● BSE (bovine spongiform encephalopathy) is the big one in the news

Humans
● Kuru
● CJD (Creutzfeldt-Jakob Disease)
● vCJD (variant Creutzfeldt-Jakob Disease). This is a distinct disease from CJD; it is almost certainly
caused by the agent that causes BSE in cattle.
● Less common but reasonably well-characterized prion diseases in humans include: FFI (fatal familial
insomnia) and GSS (Gerstmann-Straussler-Scheinker syndrome)
Elk and deer
● CWD (chronic wasting disease)

History Of Prions
In 1997, American biologist Stanley B. Prusiner
received the Nobel Prize in medicine for his
discovery of prions, “an entirely new genre of
disease-causing agents”.
Prion diseases and prions are so unusual and so

fascinating that they have been the subject of
two Nobel prizes in Physiology or Medicine.
In 1976 Carleton Gajdusek shared the Nobel

prize for his work showing that the human
disease kuru was similar to the well known sheep
disease scrapie.
In 1997 Stanley Prusiner, at UCSF, was the sole

recipient of the prize; Prusiner was responsible
for developing the modern prion model.
● Science Direct
● Biology Libre Text
REFERENCE ●
●
Science ABC
UniProt
● NCBI
● Springer Link
THANK YOU

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Prion

Presented By - Ms Anushka Srivastava

● Structure hierarchy of Prion protein

● Prion the infectious Agent

Protein Prion Expressed in E.Coli

They have a speciﬁc active site that is used to bind

This would stop the protein from being able to do its

The prion protein can

Microscopic View of a Disease Causing Protein

● BSE (bovine spongiform encephalopathy) is the big one in the news

Elk and deer

● CWD (chronic wasting disease)

Prion diseases and prions are so unusual and so

In 1976 Carleton Gajdusek shared the Nobel

In 1997 Stanley Prusiner, at UCSF, was the sole

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