2.50
Hdl Handle:
http://hdl.handle.net/10033/231813
Title:
Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.
Authors:
Raz, Assaf; Talay, Susanne R; Fischetti, Vincent A
Abstract:
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.
Affiliation:
Bacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. araz@rockefeller.edu
Citation:
Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. 2012, 84 (4):631-47 Mol. Microbiol.
Journal:
Molecular microbiology
Issue Date:
May-2012
URI:
http://hdl.handle.net/10033/231813
DOI:
10.1111/j.1365-2958.2012.08047.x
PubMed ID:
22512736
Type:
Article
Language:
en
ISSN:
1365-2958
Appears in Collections:
Publications of Dept. Medizinische Mikrobiologie (MMIK)

Full metadata record

DC FieldValue Language
dc.contributor.authorRaz, Assafen_GB
dc.contributor.authorTalay, Susanne Ren_GB
dc.contributor.authorFischetti, Vincent Aen_GB
dc.date.accessioned2012-07-03T08:40:21Z-
dc.date.available2012-07-03T08:40:21Z-
dc.date.issued2012-05-
dc.identifier.citationCellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes. 2012, 84 (4):631-47 Mol. Microbiol.en_GB
dc.identifier.issn1365-2958-
dc.identifier.pmid22512736-
dc.identifier.doi10.1111/j.1365-2958.2012.08047.x-
dc.identifier.urihttp://hdl.handle.net/10033/231813-
dc.description.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.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Molecular microbiologyen_GB
dc.titleCellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.en
dc.typeArticleen
dc.contributor.departmentBacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. araz@rockefeller.eduen_GB
dc.identifier.journalMolecular microbiologyen_GB

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