Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.
Average rating
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.
Star rating
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Issue Date
2012-05
Metadata
Show full item recordAbstract
Wall-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.Citation
Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. 2012, 84 (4):631-47 Mol. Microbiol.Affiliation
Bacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. araz@rockefeller.eduJournal
Molecular microbiologyPubMed ID
22512736Type
ArticleLanguage
enISSN
1365-2958ae974a485f413a2113503eed53cd6c53
10.1111/j.1365-2958.2012.08047.x
Scopus Count
The following license files are associated with this item: