The cytotoxic Staphylococcus aureus PSMα3 reveals a cross-α amyloid-like fibril

Einav Tayeb-Fligelman, Orly Tabachnikov, Asher Moshe, Orit Goldshmidt-Tran, Michael R. Sawaya, Nicolas Coquelle, Jacques Philippe Colletier, Meytal Landau*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Amyloids are ordered protein aggregates, found in all kingdoms of life, and are involved in aggregation diseases as well as in physiological activities. In microbes, functional amyloids are often key virulence determinants, yet the structural basis for their activity remains elusive.We determined the fibril structure and function of the highly toxic, 22-residue phenol-soluble modulin a3 (PSMa3) peptide secreted by Staphylococcus aureus. PSMa3 formed elongated fibrils that shared the morphological and tinctorial characteristics of canonical cross-b eukaryotic amyloids. However, the crystal structure of full-length PSMa3, solved de novo at 1.45 angstrom resolution, revealed a distinctive "cross-α" amyloid-like architecture, in which amphipathic a helices stacked perpendicular to the fibril axis into tight self-associating sheets.The cross-a fibrillation of PSMa3 facilitated cytotoxicity, suggesting that this assembly mode underlies function in S. aureus.

Original languageEnglish
Pages (from-to)831-833
Number of pages3
Issue number6327
StatePublished - 24 Feb 2017
Externally publishedYes


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