Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractWall-anchored surface proteins are critical for the in vivo survival of Streptococcus pyogenes. Cues in the signal sequence direct the membrane translocation of surface proteins: M protein to the septum, and SfbI to the poles. Both proteins are subsequently anchored to the wall by the membrane bound enzyme sortase A. However, the cellular features of these pathways are not fully understood. Here we show that M protein and SfbI are anchored simultaneously throughout the cell cycle. M protein is rapidly anchored at the septum, and in part of the cell cycle, is anchored simultaneously at the mother and daughter septa. Conversely, SfbI accumulates gradually on peripheral peptidoglycan, resulting in a polar distribution. Sortase is not required for translocation of M protein or SfbI at their respective locations. Methicillin-induced unbalanced peptidoglycan synthesis diminishes surface M protein but not SfbI. Furthermore, overexpression of the division regulator DivIVA also diminishes surface M protein but increases SfbI. These results demonstrate a close connection between the regulation of cell division and protein anchoring. Better understanding of the spatial regulation of surface anchoring may lead to the identification of novel targets for the development of anti-infective agents, given the importance of surface molecules for pathogenesis.
CitationCellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. 2012, 84 (4):631-47 Mol. Microbiol.
AffiliationBacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. firstname.lastname@example.org
The following license files are associated with this item:
- The M Protein of Streptococcus pyogenes Strain AP53 Retains Cell Surface Functional Plasminogen Binding after Inactivation of the Sortase A Gene.
- Authors: Russo BT, Ayinuola YA, Singh D, Carothers K, Fischetti VA, Flores-Mireles AL, Lee SW, Ploplis VA, Liang Z, Castellino FJ
- Issue date: 2020 Apr 27
- Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane.
- Authors: Raz A, Fischetti VA
- Issue date: 2008 Nov 25
- Streptococcus pyogenes Sortase Mutants Are Highly Susceptible to Killing by Host Factors Due to Aberrant Envelope Physiology.
- Authors: Raz A, Tanasescu AM, Zhao AM, Serrano A, Alston T, Sol A, Bachrach G, Fischetti VA
- Issue date: 2015
- Co-operative binding of human fibronectin to Sfbl protein triggers streptococcal invasion into respiratory epithelial cells.
- Authors: Talay SR, Zock A, Rohde M, Molinari G, Oggioni M, Pozzi G, Guzman CA, Chhatwal GS
- Issue date: 2000 Dec
- The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells.
- Authors: Molinari G, Talay SR, Valentin-Weigand P, Rohde M, Chhatwal GS
- Issue date: 1997 Apr