2020
DOI: 10.1016/j.str.2019.12.006
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Abstract: The phenol-soluble modulin (PSM) peptide family, secreted by Staphylococcus aureus, performs various virulence activities, some mediated by the formation of amyloid fibrils of diverse architectures. Specifically, PSMα1 and PSMα4 structure the S. aureus biofilm by assembling into robust cross-β amyloid fibrils. PSMα3, the most cytotoxic member of the family, assembles into cross-α fibrils in which α-helices stack into tightly mated sheets, mimicking the cross-β architecture. Here we demonstrated that massive T-… Show more

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Cited by 55 publications
(115 citation statements)
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“…In solution, uperin 3.5 formed a random-coil structure with typical minima at 197 nm, as measured using circular dichroism (CD) spectroscopy. This was in contrast to PSMα3, which is helical in solution 31 . Nevertheless, the addition of small unilamellar vesicles (SUVs) composed of 1,2dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) and 1,2-dioleoyl-sn-glycero-3-phospho-(1'rac-glycerol) (DOPG) at a 1:3 molar ratio, mimicking a Gram-positive bacterial membrane 43,44 , induced an immediate secondary structure transition of uperin 3.5 towards an α-helical conformation, with typical minima near 208 and 222 nm ( Figure 2A).…”
Section: Uperin 35 Shows a Chameleon Propensity Of A Secondary Strucmentioning
confidence: 63%
See 1 more Smart Citation
“…In solution, uperin 3.5 formed a random-coil structure with typical minima at 197 nm, as measured using circular dichroism (CD) spectroscopy. This was in contrast to PSMα3, which is helical in solution 31 . Nevertheless, the addition of small unilamellar vesicles (SUVs) composed of 1,2dioleoyl-sn-glycero-3-phosphoethanolamine (DOPE) and 1,2-dioleoyl-sn-glycero-3-phospho-(1'rac-glycerol) (DOPG) at a 1:3 molar ratio, mimicking a Gram-positive bacterial membrane 43,44 , induced an immediate secondary structure transition of uperin 3.5 towards an α-helical conformation, with typical minima near 208 and 222 nm ( Figure 2A).…”
Section: Uperin 35 Shows a Chameleon Propensity Of A Secondary Strucmentioning
confidence: 63%
“…Moreover, while PSMα3 cross-α fibrils dissolved when subjected to heat shock, uperin 3.5 was thermostable ( Figures S6 and 3B), which is likely attributed to the heat-induced transition into cross-β fibrils ( Figure 3A). In PSMα3, secondary structure changes were only inducible via mutations 31 or truncations 29 which formed mixed α/β populations or exclusively β-rich structures 31 .…”
Section: Discussionmentioning
confidence: 99%
“…These fibrils are composed entirely of α-helices that stack perpendicular to the fibril axis into mated 'sheets', just as the β-strands assemble in amyloid cross-β fibrils (31). Moreover, while PSMα3 is toxic to human cells, some of its truncations and single-point mutations show antibacterial activity (32)(33)(34)(35). Although originating from different organisms, PSMα3 and hLL-37 display sequence homology, particularly in their core region ( Fig.…”
mentioning
confidence: 99%
“…Our previous findings demonstrated cross-α fibrillation of the cytotoxic phenol-soluble modulin α3 (PSMα3) peptide secreted by the pathogenic bacterium Staphylococcus aureus. These fibrils are composed entirely of α-helices that stack perpendicular to the fibril axis into mated 'sheets', just as the β-strands assemble in amyloid cross-β fibrils (19)(20)(21). Moreover, while PSMα3 is toxic to human cells, some of its truncations and single-point mutations show antibacterial activity (22)(23)(24).…”
mentioning
confidence: 99%
“…Simiarly, the characteristic but unusual cross-α fibrils of PSMα3 are maintained in the presence of heparin [9,50]. Heparin led the non-aggregating δ-toxin peptide (which forms α-helices in solution)…”
Section: Cationic Heparin-binding Motifs In the αPsms Family May Drivmentioning
confidence: 99%