Q2. Why and how i choose my Media Assignment research topic.

Prions. An unusual pathogen.

Prions are just proteins. In fact, they are present in everyone at this very instant, perfectly harmless and contributing to normal functioning. But a mistake in the folding in the protein during gene expression causes it to change structure and become pathogenic. When it comes to acellular infectious agents, viruses are always in the spotlight. Prions are often overlooked, although they too are acellular pathogens that can cause commendable damage.

Prions can cause pathogenesis without the presence of genetic material, a property unusual to acellular viral pathogens and cellular bacterial, protozoan and fungal pathogens.

The other amazing fact about their action is that not only do the mis-folded mutated prion directly affect body tissue, but they can also cause normal proteins to change their structure and in-turn become pathogenic.

I think a driving factor in choosing this topic has been that prion pathogenesis is not covered in the PATH2201 course theory. However, my interest in prions was piqued when I had watched a documentary in high school- we were introduced to the case of the Mad Cow disease outbreak in the UK- a case where a disease previously known in cattle like cows (Bovine Spongiform Encephalopathy)  made its way to humans. This was done by people ingesting meat contaminated with pathogenic prions of ailing cows- which had somehow slipped past authorities and ended up in food circulation.

In humans, the disease is called Creutzfeldt-Jakob disease (CJD) and is degenerative brain disorder which is fatal- the multiplication of prion proteins leads to the formation of holes in the brain, leading to loss of normal functioning and thought. Death follows.prions1

This disease is thought to be incurable- until recent research looking into creating anti-prion drugs that function by inactivating protein aggregation (the process that causes holes) and hence using them to slow the progress of the disease. These experiments are the main focus on my report which seeks to address how prions can be blocked by anti-prion chemicals, and how further research in this area is crucial.

Writing this report on prion disease is relevant-especially in the wake of identifying Multiple System Atrophy (MSA), a neurodegenerative disease, as being caused by prions. This identification of a new prion has led to questions about whether neurodegenerative diseases have similar pathogenesis to prions and are in fact linked to prions. This speculation is not unusual- considering that most neurodegenerative disorders pathogenesis is not fully understood.

A way to test this speculation and simultaneously find a cure for neurodegenerative diseases, would be to explore anti-prion drugs and get them available for clinical trials. I feel like we are on the cusp of something grand- if we do find a correlation between prions and degenerative disorders, and develop appropriate drugs to cure them- this will definitely change the face of neuronal medicine, enabling the human mortality rate to no longer be deterred by neurodegeneration.

This is the basis of my research article. I aim to start researching the Cruedtzfeld Jacob’s disease and analyze the experiments done to counter-act the pathogenic prions- the limitations and possibilities of the anti prion drugs used and scope for further improvement.

These are my ideas so far- but considering the beauty of science, it is subject to modification as I acquire new information- I will, obviously, keep everyone updated with the details.

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