Lookup NU author(s): Dr Alexandra Solovyova,
Dr Paul Race,
Dr Wendy Smith,
Professor Michael Kehoe,
Dr Mark Banfield
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Solovyova AS, Pointon JA, Race PR, Smith WD, Kehoe MA, Banfield MJ
Publication type: Article
Publication status: Published
Journal: European Biophysics Journal
ISSN (print): 0175-7571
ISSN (electronic): 1432-1017
Altmetrics provided by Altmetric