UPSC MainsBOTANY-PAPER-I202310 Marks150 Words
Q1.

What are prions? How do they differ from viruses? Mention few diseases caused by prions in animals and human beings.

How to Approach

This question requires a clear understanding of prions, their unique characteristics, and how they differ from viruses. The answer should define prions, highlight their composition (or lack thereof of nucleic acids), and contrast them with the structure of viruses. Mentioning specific diseases caused by prions in both animals and humans is crucial. A comparative table can be used to effectively illustrate the differences between prions and viruses. The answer should be concise, sticking to the 150-word limit.

Model Answer

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Introduction

Prions are unique infectious agents, distinct from conventional pathogens like bacteria, viruses, fungi, and parasites. The term "prion" stands for "proteinaceous infectious particle," coined by Stanley Prusiner, who received the Nobel Prize in Physiology or Medicine in 1997 for their discovery. Unlike other infectious agents, prions lack nucleic acids (DNA or RNA) and are composed solely of misfolded proteins. These misfolded proteins have the ability to induce normal proteins to adopt the same aberrant conformation, leading to a cascade of misfolding and ultimately causing disease.

Prions: Structure and Mechanism

Prions are infectious isoforms of normal cellular proteins found predominantly in the nervous system. The normal, harmless form is denoted as PrPC (cellular prion protein), while the misfolded, infectious form is PrPSc (scrapie prion protein). PrPSc induces PrPC to convert into PrPSc, leading to aggregation and neuronal damage.

Prions vs. Viruses

The key difference lies in their composition. Viruses contain nucleic acid (DNA or RNA) enclosed within a protein coat, requiring a host cell for replication. Prions, however, are solely protein and replicate by converting normal proteins into the misfolded form.

Feature Prions Viruses
Composition Misfolded protein (PrPSc) Nucleic acid (DNA or RNA) + Protein coat
Replication Conversion of PrPC to PrPSc Host cell machinery
Antibiotic/Antiviral Sensitivity Resistant Sensitive to antivirals

Diseases Caused by Prions

  • Animals: Scrapie (sheep), Bovine Spongiform Encephalopathy (BSE or "mad cow disease" in cattle), Chronic Wasting Disease (CWD) in deer and elk.
  • Humans: Creutzfeldt-Jakob Disease (CJD), Variant Creutzfeldt-Jakob Disease (vCJD) linked to BSE, Gerstmann-Sträussler-Scheinker syndrome (GSS), Fatal Familial Insomnia (FFI).

Conclusion

Prions represent a unique class of infectious agents, posing significant challenges due to their unconventional nature and resistance to conventional sterilization methods. Their ability to induce protein misfolding and cause devastating neurodegenerative diseases highlights the importance of understanding their mechanisms and developing effective prevention and treatment strategies. Continued research is crucial to combat these rare but invariably fatal conditions.

Answer Length

This is a comprehensive model answer for learning purposes and may exceed the word limit. In the exam, always adhere to the prescribed word count.

Additional Resources

Key Definitions

Prion
A misfolded protein capable of transmitting its structural conformation to other proteins, leading to a chain reaction of misfolding and disease.
PrP<sup>Sc</sup>
The scrapie prion protein, the misfolded, infectious isoform of the prion protein. It is resistant to proteases and tends to aggregate.

Key Statistics

vCJD, linked to BSE, peaked in the UK in 2000 with 180 cases reported, and has since declined significantly due to control measures.

Source: Public Health England (as of knowledge cutoff 2021)

CJD has an estimated incidence of 1-2 cases per million people per year globally.

Source: World Health Organization (as of knowledge cutoff 2021)

Examples

Mad Cow Disease (BSE)

BSE in cattle originated from feeding cattle meat and bone meal contaminated with prion proteins from scrapie-infected sheep. This led to a public health crisis when it was linked to vCJD in humans.

Kuru

Kuru is a prion disease historically found among the Fore people of Papua New Guinea, caused by the consumption of brains of deceased relatives as part of ritualistic cannibalism.

Frequently Asked Questions

Are prions living?

Prions are not considered living organisms as they lack nucleic acids and cannot reproduce independently. They are infectious agents, but their mode of replication differs significantly from that of viruses or bacteria.

Is there a cure for prion diseases?

Currently, there is no cure for prion diseases. Treatment is largely supportive, focusing on managing symptoms and improving quality of life. Research is ongoing to develop therapies that can prevent prion conversion or clear existing prions.

Topics Covered

BiologyMicrobiologyMedicinePrionsVirusesInfectious DiseasesPathology