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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/134884
Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis
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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, " - ", 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 amyloid assemblies. To investigate this
possibility, we performed a stringent computational survey for
Q/N-rich PrLDs on " - ". Our data indicate that \xE2\x88\xBC10%
of " - " protein sequences have prionic signatures, and that
this subproteome is enriched in regulatory proteins, such as
transcription factors and RNA-binding proteins. Furthermore, we
experimentally demonstrate for several of the identified PrLDs
that, despite their disordered nature, they contain inner short
sequences able to spontaneously self-assemble into amyloid-like
structures. Although the ability of these sequences to nucleate
the conformational conversion of the respective full-length
proteins should still be demonstrated, our analysis suggests
that, as previously described for other organisms, prion-like
proteins might also play a functional role in P. falciparum.
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PALLARÈS, Irantzu, et al. Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis. Frontiers in Microbiology. 2018. Vol. 9. ISSN 1664-302X. [consulted: 17 of October of 2026]. Available at: https://hdl.handle.net/2445/134884