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...Obviously, something very significant is taking place. Most of these fungal diseases have only appeared in the past 30 years. I've read all of the various causation theories...climate change, pesticide use, GMOs, human population and mobility....but the truth is, no one really seems to know for sure. Maybe it's a combination of all-of-the-above.
One thing is certain, however, the environmental, health and economic toll is huge........and growing.
....Brave new world....
Prions can improve the health of fungal populations
Prions, infectious agents composed of proteins with a specific misfolded and transmissible 3D structure that cuases diseases like BSE, can be present in fungal populations on a large scale, preventing the spread of fungal parasites and keeping the population relatively healthy. This remarkable discovery was published in this week’s edition of the scientific magazine PNAS by scientists from Wageningen University, part of Wageningen UR. What makes the findings so extraordinary is that many scientists had previously assumed that prions had only a negative effect on the health of their ‘host’.
Prions of Fungi: Inherited Structures and Biological Roles
The term 'prion' means an infectious protein that does not need an accompanying nucleic acid. There are six fungal prions, including four self-propagating amyloids and two enzymes that are necessary to activate their inactive precursors. Here we explore the scope of the prion phenomenon, the biological and evolutionary roles of prions, the structural basis of the amyloid prions, and the prominent role of chaperones (proteins that affect the folding of other proteins) and other cellular components in prion generation and propagation.
High natural prevalence of a fungal prion
Prions are infectious proteinaceous particles. Prions were first identified in mammals as the causal agents of a group of fatal neurodegenerative diseases termed spongiform encephalopathies including Scrapie, BSE, and Creutzfeldt-Jakob disease (1, 2). Many prion proteins were also identified in fungi, especially in the yeast S. cerevisiae (3). Currently, ∼10 fungal prion proteins have been identified and 19 additional candidates await further characterization (4–6).
originally posted by: loam
a reply to: soficrow
It looks like all of the ways fungi and prions interact is still pretty unclear.
Do you think their interaction may also play a role in prion replication?
originally posted by: _damon
the earth might be creating new diseases and microorganisms that would drive mankind to extinction or severerly reduce it. As well as cataclysms. Take it the same way as a diseased body who reacts to pathogens and intruders by finding ways to eradicate them, without consideration of their own existences or perspectives (they got one, to be sure), the goal being solely to protect itself and heal. As above, so below.
Its only hypothetic of course but the odds are high.
Prog Mol Biol Transl Sci. 2012;107:417-56. doi: 10.1016/B978-0-12-385883-2.00007-2.
Staniforth GL1, Tuite MF.
For both mammalian and fungal prion proteins, conformational templating drives the phenomenon of protein-only infectivity. The conformational conversion of a protein to its transmissible prion state is associated with changes to host cellular physiology. In mammals, this change is synonymous with disease, whereas in fungi no notable detrimental effect on the host is typically observed. Instead, fungal prions can serve as epigenetic regulators of inheritance in the form of partial loss-of-function phenotypes. In the presence of environmental challenges, the prion state [PRION(+)], with its resource for phenotypic plasticity, can be associated with a growth advantage. The growing number of yeast proteins that can switch to a heritable [PRION(+)] form represents diverse and metabolically penetrating cellular functions, suggesting that the [PRION(+)] state in yeast is a functional one, albeit rarely found in nature. In this chapter, we introduce the biochemical and genetic properties of fungal prions, many of which are shared by the mammalian prion protein PrP, and then outline the major contributions that studies on fungal prions have made to prion biology.
Copyright © 2012 Elsevier Inc. All rights reserved.
Interaction of Human Laminin Receptor with Sup35, the [PSI+] Prion-Forming Protein from S. cerevisiae: A Yeast Model for Studies of LamR Interactions with Amyloidogenic Proteins
The laminin receptor (LamR) is a cell surface receptor for extracellular matrix laminin, whereas the same protein within the cell interacts with ribosomes, nuclear proteins and cytoskeletal fibers. LamR has been shown to be a receptor for several bacteria and viruses. Furthermore, LamR interacts with both cellular and infectious forms of the prion protein, PrPC and PrPSc. ...
...Sup35, a yeast prion-forming protein that has been extensively studied, is a translational termination factor (eRF3) in its soluble form , . However, when aggregated as a prion , , [PSI+], Sup35 is unavailable to terminate protein synthesis. Under this condition, protein termination is suppressed as ribosomes occasionally read through stop codons. ...
...Evidence ....reveal an interaction between LamR and Sup35 in [PSI+] cells, indicating that LamR interacts with Sup35-based prion protein.