Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis.

ABSTRACT: Prions are a singular subset of proteins able to switch between a soluble conformation and a self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases, increasing evidence indicates that organisms exploit prion-like mechanisms for beneficial purposes. The ability to transit between conformations is encoded in the so-called prion domains, long disordered regions usually enriched in glutamine/asparagine residues. Interestingly, Plasmodium falciparum, the parasite that causes the most virulent form of malaria, is exceptionally rich in proteins bearing long Q/N-rich sequence stretches, accounting for roughly 30% of the proteome. This biased composition suggests that these protein regions might correspond to prion-like domains (PrLDs) and potentially form

SUBMITTER: Pallares I 

PROVIDER: S-EPMC6090025 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature