Title |
Prions in Microbes: The Least in the Most |
Author |
Moonil Son1,2,3*, Sia Han2, and Seyeon Lee2 |
Address |
1Department of Microbiology, Pusan National University, Busan 46241, Republic of Korea, 2Department of Integrated Biological Science, Pusan National University, Busan 46241, Republic of Korea, 3Microbiological Resource Research Institute, Pusan National University, Busan 46241, Republic of Korea |
Bibliography |
Journal of Microbiology, 61(10),881-889, 2023,
|
DOI |
10.1007/s12275-023-00070-4
|
Key Words |
Prion · Amyloid · Yeast · Fungi · Bacteria · Anti-prion system |
Abstract |
Prions are infectious proteins that mostly replicate in self-propagating amyloid conformations (filamentous protein polymers)
and consist of structurally altered normal soluble proteins. Prions can arise spontaneously in the cell without any
clear reason and are generally considered fatal disease-causing agents that are only present in mammals. However, after the
seminal discovery of two prions, [PSI+] and [URE3], in the eukaryotic model microorganism Saccharomyces cerevisiae,
at least ten more prions have been discovered, and their biological and pathological effects on the host, molecular structure,
and the relationship between prions and cellular components have been studied. In a filamentous fungus model, Podospora
anserina, a vegetative incomparability-related [Het-s] prion that directly triggers cell death during anastomosis (hyphal
fusion) was discovered. These prions in eukaryotic microbes have extended our understanding to overcome most fatal human
prion/amyloid diseases. A prokaryotic microorganism (Clostridium botulinum) was reported to have a prion analog. The
transcriptional regulators of C. botulinum-Rho can be converted into the self-replicating prion form ([RHO-X-C+]), which
may affect global transcription. Here, we outline the major issues with prions in microbes and the lessons learned from the
relatively uncovered microbial prion world. |