Viroids, virusoids, and prions are unique infectious agents that challenge our understanding of life. These tiny pathogens lack traditional cellular structures yet can cause devastating diseases in plants and animals.
Unlike viruses, these agents have simpler structures and replication methods. Viroids and virusoids are small RNA molecules, while prions are misfolded proteins. Their ability to replicate and spread without typical genetic material makes them fascinating subjects in microbiology.
Viroids, Virusoids, and Prions
Structure and replication of viroids
- Smallest known infectious agents consist solely of a single-stranded, circular RNA molecule without a protein coat, unlike viruses
- Genome size ranges from 246 to 467 nucleotides (potato spindle tuber viroid, chrysanthemum stunt viroid)
- Replication occurs in the nucleus of host plant cells
- Involves the RNA-dependent RNA polymerase (RdRP) of the host
- (+) strand viroid RNA acts as a template for synthesizing (-) strand RNA
- (-) strand RNA then serves as a template for synthesizing new (+) strand RNA
- Newly synthesized (+) strand RNA molecules are cleaved and circularized to form mature viroids
- Viroids lack a protein coat, have a much smaller genome, and do not encode any proteins, distinguishing them from viruses
- Some viroids possess ribozyme activity, allowing them to catalyze their own cleavage during replication
Virusoids vs satellite viruses
- Virusoids are small, circular, single-stranded RNA molecules dependent on helper viruses for replication
- Genome size ranges from 220 to 388 nucleotides (hepatitis delta virusoid, velvet tobacco mottle virusoid)
- Encapsidated within the coat protein of the helper virus
- Satellite viruses also depend on helper viruses for replication but have larger genomes (800 to 1,400 nucleotides) and encode their own coat protein (satellite tobacco necrosis virus, satellite panicum mosaic virus)
- Both virusoids and satellite viruses rely on the replication machinery of the helper virus, which provides necessary enzymes like RdRP
- They compete with the helper virus for replication resources
Prions and neurodegenerative diseases
- Infectious agents composed solely of misfolded proteins, lacking nucleic acids
- Misfolded form of the prion protein denoted as PrP$^{Sc}$ (scrapie)
- Normal cellular form of the prion protein denoted as PrP$^C$
- Prion replication and propagation involves PrP$^{Sc}$ acting as a template, inducing misfolding of normal PrP$^C$ proteins
- Misfolded PrP$^{Sc}$ proteins aggregate and accumulate in the brain, leading to neurodegeneration
- Prions cause several neurodegenerative diseases in humans and animals (transmissible spongiform encephalopathies)
- Human diseases: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Kuru
- Animal diseases: bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep
- Mechanisms of prion-induced neurodegeneration
- Accumulation of misfolded PrP$^{Sc}$ proteins leads to amyloid plaque formation
- Neuronal loss and synaptic dysfunction occur due to toxic effects of misfolded prions
- Activation of glial cells and neuroinflammation contribute to disease progression
RNA processing in viroids and virusoids
- RNA splicing plays a crucial role in the life cycle of some viroids and virusoids
- Self-cleavage and ligation of RNA molecules are essential for replication and maturation
- Hammerhead ribozymes found in certain viroids and virusoids catalyze specific RNA cleavage reactions