SynBio and the Boundaries between Functional and Pathogenic RepA-WH1 Bacterial Amyloids.
RepA-WH1
bacterial amyloids
prions
protein engineering
synthetic biology
Journal
mSystems
ISSN: 2379-5077
Titre abrégé: mSystems
Pays: United States
ID NLM: 101680636
Informations de publication
Date de publication:
30 Jun 2020
30 Jun 2020
Historique:
entrez:
2
7
2020
pubmed:
2
7
2020
medline:
2
7
2020
Statut:
epublish
Résumé
Amyloids are protein polymers that were initially linked to human diseases. Across the whole Tree of Life, many disease-unrelated proteins are now emerging for which amyloids represent distinct functional states. Most bacterial amyloids described are extracellular, contributing to biofilm formation. However, only a few have been found in the bacterial cytosol. This paper reviews from the perspective of synthetic biology (SynBio) our understanding of the subtle line that separates functional from pathogenic and transmissible amyloids (prions). In particular, it is focused on RepA-WH1, a functional albeit unconventional natural amyloidogenic protein domain that participates in controlling DNA replication of bacterial plasmids. SynBio approaches, including protein engineering and the design of allosteric effectors such as diverse ligands and an optogenetic module, have enabled the generation in RepA-WH1 of an intracellular cytotoxic prion-like agent in bacteria. The synthetic RepA-WH1 prion has the potential to develop into novel antimicrobials.
Identifiants
pubmed: 32606029
pii: 5/3/e00553-20
doi: 10.1128/mSystems.00553-20
pmc: PMC7329326
pii:
doi:
Types de publication
Journal Article
Review
Langues
eng
Informations de copyright
Copyright © 2020 Giraldo.
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