Evidence map›Paper›PMID 26811319›Full record

ArticleJournal of bacteriology2016

SagB Glucosaminidase Is a Determinant of Staphylococcus aureus Glycan Chain Length, Antibiotic Susceptibility, and Protein Secretion.

Yvonne G Y Chan, Matthew B Frankel, Dominique Missiakas, Olaf Schneewind

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

35 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Mutation of lipoprotein processing pathway geneAntimicrobial agents and chemotherapy · 2026
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  5. Peptidoglycan polymerase function and regulation.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  6. Article
  7. Article
  8. The Secondary Resistome of Methicillin-ResistantAntibiotics (Basel, Switzerland) · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Microbiology spectrum · 2023
    Article
  15. Identification of FacZ as a division site placement factor inbioRxiv : the preprint server for biology · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 2 institutions in 1 country.

Yvonne G Y ChanDepartment of Microbiology, University of Chicago, Chicago, Illinois, USA.
Matthew B FrankelDepartment of Microbiology, University of Chicago, Chicago, Illinois, USA.
Dominique MissiakasDepartment of Microbiology, University of Chicago, Chicago, Illinois, USA Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Argonne, Illinois, USA.
Olaf SchneewindDepartment of Microbiology, University of Chicago, Chicago, Illinois, USA Howard Taylor Ricketts Laboratory, Argonne National Laboratory, Argonne, Illinois, USA oschnee@bsd.uchicago.edu.
University of Chicago · USArgonne National Laboratory · US

Funding

Surface Proteins of Gram-Positive BacteriaR01AI038897 · NIAID · UNIVERSITY OF CHICAGO · PI MISSIAKAS, DOMINIQUE M. · 1996 to 2024
$8.9M
Vaccine Assembly from Surface Proteins of Staphylococcus AureusR01AI052474 · NIAID · UNIVERSITY OF CHICAGO · PI Dominique Missiakas · 2002 to 2026
$8.8M
Characterization of the secretion pathways for surface proteins in S. AureusF32AI085709 · NIAID · UNIVERSITY OF CHICAGO · PI FRANKEL, MATTHEW · 2010 to 2012
$153k
NIAID NIH HHS AI038897NIAID NIH HHS AI052474NIAID NIH HHS F32 AI085709NIAID NIH HHS F32AI085709NIAID NIH HHS R01 AI038897NIAID NIH HHS R01 AI052474
6 · The paper itself

Abstract

unlabelledThe envelope of Staphylococcus aureus is comprised of peptidoglycan and its attached secondary polymers, teichoic acid, capsular polysaccharide, and protein. Peptidoglycan synthesis involves polymerization of lipid II precursors into glycan strands that are cross-linked at wall peptides. It is not clear whether peptidoglycan structure is principally determined during polymerization or whether processive enzymes affect cell wall structure and function, for example, by generating conduits for protein secretion. We show here that S. aureus lacking SagB, a membrane-associated N-acetylglucosaminidase, displays growth and cell-morphological defects caused by the exaggerated length of peptidoglycan strands. SagB cleaves polymerized glycan strands to their physiological length and modulates antibiotic resistance in methicillin-resistant S. aureus (MRSA). Deletion of sagB perturbs protein trafficking into and across the envelope, conferring defects in cell wall anchoring and secretion, as well as aberrant excretion of cytoplasmic proteins. IMPORTANCE: Staphylococcus aureus is thought to secrete proteins across the plasma membrane via the Sec pathway; however, protein transport across the cell wall envelope has heretofore not been studied. We report that S. aureus sagB mutants generate elongated peptidoglycan strands and display defects in protein secretion as well as aberrant excretion of cytoplasmic proteins. These results suggest that the thick peptidoglycan layer of staphylococci presents a barrier for protein secretion and that SagB appears to extend the Sec pathway across the cell wall envelope.

Indexed as

Drug Resistance, BacterialAmino Acid SequenceAnti-Bacterial AgentsBacterial ProteinsGene Expression Regulation, BacterialHexosaminidasesMolecular Sequence DataMutationPolysaccharidesStaphylococcus aureusAnti-Bacterial AgentsBacterial ProteinsHexosaminidasesPolysaccharides

Identifiers

PMID26811319
PMCPMC4800868
OpenAlexW2255866615

What OpenQuestion holds

Textmetadata
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.