Evidence map›Paper›PMID 22512736›Full record

ArticleMolecular microbiology2012

Cellular aspects of the distinct M protein and SfbI anchoring pathways in Streptococcus pyogenes.

Assaf Raz, Susanne R Talay, Vincent A Fischetti

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.5field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Surface Proteins on Gram-Positive Bacteria.Microbiology spectrum · 2019
    Review
  7. Article
  8. Lysibodies are IgG Fc fusions with lysin binding domains targetingProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. The elongation of ovococci.Microbial drug resistance (Larchmont, N.Y.) · 2014
    Review
  12. Dual defensin strategy for targeting Enterococcus faecalis.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Assaf RazBacterial Pathogenesis and Immunology, Rockefeller University, New York, USA. araz@rockefeller.edu
Susanne R Talay
Vincent A Fischetti
Rockefeller University · USHelmholtz Centre for Infection Research · DE

Funding

PROPERTIES OF STREPTOCOCCAL M PROTEINR37AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1987 to 2006
$2.7M
PROPERTIES OF STREPTOCOCCAL M PROTEINR01AI011822 · NIAID · ROCKEFELLER UNIVERSITY · PI FISCHETTI, VINCENT A. · 1985 to 2011
$1.7M
NIAID NIH HHS AI11822NIAID NIH HHS R01 AI011822NIAID NIH HHS R37 AI011822
6 · The paper itself

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.

Indexed as

Cell DivisionAdhesins, BacterialAminoacyltransferasesAntigens, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsCysteine EndopeptidasesPeptidoglycanStreptococcus pyogenesAdhesins, BacterialAminoacyltransferasesAntigens, BacterialBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsCysteine Endopeptidasesfibronectin-binding proteins, bacterialPeptidoglycansortase Astreptococcal M protein

Identifiers

PMID22512736
PMCPMC3383811
OpenAlexW2140007477

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.