The Biochemistry of Bovine

Spongiform Encephalopathy
(BSE)
Otherwise Known as Mad Cow Disease

Model of an Essential Amino

Acid

Two Chemical Characteristics of

Methionine

The sulfur group thiol is prone to oxidation.

Hydrophobic.
(Arizona)

Levels of Protein Structure

Dehydration Synthesis and the

Formation of a Peptide Bond

Two amino acids

are joined
together by a
peptide bond.
During this
process the
glycine loses an
OH from its
carboxyl group
and Alanine
loses it H from
its amine group
forming water or

Hydrolysis and the Breaking of

the Peptide Bond
The peptide bond
is broken when
water or H2O is
added to a
polypeptide.
The OH will go to
the carboxyl group
of the Glycine and
the H will go to the
amine group of the
alanine to
complete the two
amino acids.

Four Forces that stabilize a Proteins

Three-Dimensional Structure

Hydrophobic Interactions
Hydrogen Bonds
Ionic Bonding
Disulfide Bridges

Hydrophobic Interactions
Hydrophobic Interactions are the clustering
of hydrophobic R groups in the center of the
molecule to minimize contact with water.

Hydrogen Bonds
A hydrogen bond forms when two atoms are
electrostatically attracted to each other
between molecules.
When the two molecules are in side amino
acid chains, the tertiary structure is
stabilized.
Amino acids with oxygen or nitrogen will
form these hydrogen bonds.

Ionic Bonding
An electrostatic attraction between two polar
side amino acid chains help stabilize the
structure at the core of the protein.

Disulfide Bridges
A strong force created when two cysteine
side groups form a covalent bond.

The Role of Prions in BSE

Prions are proteins that occur naturally in a cell
membrane and are designated PrPc.
Infected prions are designated PrPsc and have the
same amino acid sequence as PrPc, but are
shaped differently.
The PrPscs enter through infected feed that is
made from other animals.
The PrPscs will convert PrPcs into PrPscs.
(Hudon-Miller)

Protein Misfolding and

Aggregation in BSE
Misfolding causes a changes in the protein,
making it hydrophobic and unable to function
normally.
The infected protein (PrPsc) acts as a
chaperone and infects other PrPcs.
The infected PrPcs cannot do their job in the cell
so the cell produces more PrPcs to do the job.
As more are produced, more get infected.
(Hudon-Miller)

Protein Misfolding and

Aggregation in BSE
The infected PrPc are not recognized by the
Proteasomes and are not eliminated by the
cell.
The infected PrPcs build up and begin to
aggregate or stick together.
This aggregation and build up of infected
PrPcs eventually leads to cell death.
As cells die within tissue, the place of the
cell is not filled creating sponge like holes.
(Hudon-Miller)

Role of the Chaperone

Protein
The role of a normal chaperone is to enable
proteins to fold normally.
PrPscs will act as a chaperone to cause the
misfolding in PrPcs allowing them to become
PrPscs.
Normal chaperones have no effect on the
PrPscs so they cannot fix or transform the
PrPscs back to PrPcs.
(Hudon-Miller)

How Can the USA Decrease the

Risk of BSE in the Food Supply
Prohibit the inclusion of brain and spinal cord tissue in
feed.
Removal of brain and spinal cord tissue at slaughter and
processing.
Surveillance of occurrences of neurological disorders.
Awareness programs to aid surveillance.
Screening tests at slaughter.
Destruction of animals exposed to contaminated feed.
Appropriate disposal of carcasses and animal byproducts.
(OIE)

References
Clark, J (2012) The Structure of Proteins. Chemguide. March
27, 2014 from http://
www.chemguide.co.uk/organicprops/aminoacids/proteinstru
ct.html
OIE, (2014) Prevention and Control. OIE, World Organisation
for Animal Health. March 28, 2014 from http
://www.oie.int/animal-health-in-the-world/bse-portal/preven
tion-and-control
/
Arizona (2003) Methionine. The Biology Project. March 23,
2014 from http://
www.biology.arizona.edu/biochemistry/problem_sets/aa/Met
hionine.html
Hudon-Miller, S. (2012) Bovine spongiform encephalopathy.
March 27, 2014 from http://youtu.be/TE8e5rRreSE