ArticleEuropean biophysics journal : EBJ2010
Solution structure of the major (Spy0128) and minor (Spy0125 and Spy0130) pili subunits from Streptococcus pyogenes.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- A structural snapshot of type II pilus formation in Streptococcus pneumoniae.The Journal of biological chemistry · 2015Article
- Structural model for covalent adhesion of the Streptococcus pyogenes pilus through a thioester bond.The Journal of biological chemistry · 2014Article
- Isopeptide bonds mechanically stabilize spy0128 in bacterial pili.Biophysical journal · 2013Article
- Polyproline and triple helix motifs in host-pathogen recognition.Current protein & peptide science · 2012Review
- Roles of minor pilin subunits Spy0125 and Spy0130 in the serotype M1 Streptococcus pyogenes strain SF370.Journal of bacteriology · 2010Article
- Crystal structure of the minor pilin FctB reveals determinants of Group A streptococcal pilus anchoring.The Journal of biological chemistry · 2010Article
- Purification, crystallization and preliminary crystallographic analysis of the minor pilin FctB from Streptococcus pyogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Adhesion of the serotype M1 Streptococcus pyogenes strain SF370 to human tonsil explants and cultured keratinocytes requires extended polymeric surface structures called pili. In this important human pathogen, pili are assembled from three protein subunits: Spy0125, Spy0128 and Spy0130 through the action of sortase enzymes. For this study, the structural properties of these pili proteins have been investigated in solution. Spy0125 and Spy0128 display characteristics of globular, folded proteins. Circular dichroism suggests a largely beta-sheet composition for Spy0128 and Spy0125; Spy0130 appears to contain little secondary structure. Each of the proteins adopts a monodisperse, monomeric state in solution as assessed by analytical ultracentrifugation. Further, small-angle X-ray scattering curves for Spy0125, Spy0128 and Spy0130 suggest each protein adopts an elongated shape, likely comprised of two domains, with similar maximal dimensions. Based on the scattering data, dummy atom models of each of the pili subunits have been reconstructed ab initio. This study provides the first insights into the structure of Streptococcus pyogenes minor pili subunits, and possible implications for protein function are discussed.
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