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Publication Abstract from PubMed

SignificanceThe formation of cross-alpha amyloids has been shown by crystallographic analysis of the highly cytolytic peptide PSMalpha3, a secreted virulence factor associated with the human pathogen Staphylococcus aureus. However, the relationship of the crystallographic cross-alpha structure to self-assembled filaments of PSMalpha3 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 PSMalpha3 and PSMbeta2 peptides in aqueous solution. In each case, the nanotubes are derived from self-association of cross-alpha amyloid protofilaments. The self-assembly behavior of S. aureus PSMalpha3 and PSMbeta2 peptides provides strong evidence for the importance of the cross-alpha fold in self-assembled peptide and protein structures in general and for PSMs in particular.

Phenol-soluble modulins PSMalpha3 and PSMbeta2 form nanotubes that are cross-alpha amyloids.,Kreutzberger MAB, Wang S, Beltran LC, Tuachi A, Zuo X, Egelman EH, Conticello VP Proc Natl Acad Sci U S A. 2022 May 17;119(20):e2121586119. doi:, 10.1073/pnas.2121586119. Epub 2022 May 9. PMID:35533283^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.