Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMα peptides

Nir Salinas, Jacques-Philippe Colletier, Asher Moshe and Meytal Landau ()
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Nir Salinas: Technion-Israel Institute of Technology
Jacques-Philippe Colletier: Commissariat à l’énergie atomique et aux énergies alternatives (CEA)
Asher Moshe: Technion-Israel Institute of Technology
Meytal Landau: Technion-Israel Institute of Technology

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract Members of the Staphylococcus aureus phenol-soluble modulin (PSM) peptide family are secreted as functional amyloids that serve diverse roles in pathogenicity and may be present as full-length peptides or as naturally occurring truncations. We recently showed that the activity of PSMα3, the most toxic member, stems from the formation of cross-α fibrils, which are at variance with the cross-β fibrils linked with eukaryotic amyloid pathologies. Here, we show that PSMα1 and PSMα4, involved in biofilm structuring, form canonical cross-β amyloid fibrils wherein β-sheets tightly mate through steric zipper interfaces, conferring high stability. Contrastingly, a truncated PSMα3 has antibacterial activity, forms reversible fibrils, and reveals two polymorphic and atypical β-rich fibril architectures. These architectures are radically different from both the cross-α fibrils formed by full-length PSMα3, and from the canonical cross-β fibrils. Our results point to structural plasticity being at the basis of the functional diversity exhibited by S. aureus PSMαs.

Date: 2018
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DOI: 10.1038/s41467-018-05490-0

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