Proceedings of the National Academy of Sciences | VOL. 119
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Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids

Publication Date May 9, 2022

Abstract

Significance The formation of cross-α amyloids has been shown by crystallographic analysis of the highly cytolytic peptide PSMα3, a secreted virulence factor associated with the human pathogen Staphylococcus aureus . However, the relationship of the crystallographic cross-α structure to self-assembled filaments of PSMα3 and its relevance to other phenol-soluble modulin (PSM) peptides remained an open question. We report the cryo–electron microscopy structural analysis of three nanotubes derived from self-assembly of PSMα3 and PSMβ2 peptides in aqueous solution. In each case, the nanotubes are derived from self-association of cross-α amyloid protofilaments. The self-assembly behavior of S. aureus PSMα3 and PSMβ2 peptides provides strong evidence for the importance of the cross-α fold in self-assembled peptide and protein structures in general and for PSMs in particular.

Concepts

Peptides In Aqueous Solution Phenol-soluble Modulin Self-assembled Peptide Formation Of Amyloids Protein Structures Self-assembled Protein Aqueous Solution Relationship Of Structure Self-assembled Structures Peptide Structures

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