Evidence map›Paper›PMID 24255971›Full record

ArticleACS chemical biology2014

Moenomycin resistance mutations in Staphylococcus aureus reduce peptidoglycan chain length and cause aberrant cell division.

Yuriy Rebets, Tania Lupoli, Yuan Qiao, Kathrin Schirner, Regis Villet, David Hooper, Daniel Kahne, Suzanne Walker

Abstract read
In one paragraph

Article in ACS chemical biology, 2014. 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
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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Demonstration of the role of cell wall homeostasis inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Antimicrobial agents and chemotherapy · 2020
    Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. BAL Fluid Metaproteome in Acute Respiratory Failure.American journal of respiratory cell and molecular biology · 2018
    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

8 authors at 2 institutions in 1 country.

Yuriy RebetsDepartment of Microbiology and Immunobiology, Harvard Medical School , Boston, Massachusetts 02115, United States.
Tania Lupoli
Yuan Qiao
Kathrin Schirner
Regis Villet
David Hooper
Daniel Kahne
Suzanne Walker
Harvard University · USMassachusetts General Hospital · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI RIDER, TODD H. · 2003 to 2013
$113.7M
Technical Mother Machine CoreP01AI083214 · NIAID · SCHEPENS EYE RESEARCH INSTITUTE · PI Johan Paulsson · 2009 to 2026
$39.4M
Studies Toward Hybrid Glycopeptide AntibioticsR01GM066174 · NIGMS · PRINCETON UNIVERSITY · PI KAHNE, DANIEL · 2002 to 2018
$8.9M
Mechanism and Inhibition of Enzymes that Assemble Bacterial Cell WallR01GM076710 · NIGMS · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2007 to 2019
$5.9M
NIAID NIH HHS AI057159NIAID NIH HHS AI083214NIAID NIH HHS P01 AI083214NIAID NIH HHS U54 AI057159NIGMS NIH HHS GM076710NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

Staphylococcus aureus is a Gram-positive pathogen with an unusual mode of cell division in that it divides in orthogonal rather than parallel planes. Through selection using moenomycin, an antibiotic proposed to target peptidoglycan glycosyltransferases (PGTs), we have generated resistant mutants containing a single point mutation in the active site of the PGT domain of an essential peptidoglycan (PG) biosynthetic enzyme, PBP2. Using cell free polymerization assays, we show that this mutation alters PGT activity so that much shorter PG chains are made. The same mutation in another S. aureus PGT, SgtB, has a similar effect on glycan chain length. Moenomycin-resistant S. aureus strains containing mutated PGTs that make only short glycan polymers display major cell division defects, implicating PG chain length in determining bacterial cell morphology and division site placement.

Indexed as

Drug Resistance, BacterialAnti-Bacterial AgentsBacterial ProteinsHumansModels, MolecularOligosaccharidesPeptidoglycanPeptidoglycan GlycosyltransferasePoint MutationProtein Structure, TertiaryStaphylococcal InfectionsStaphylococcus aureusAnti-Bacterial AgentsBacterial ProteinsmoenomycinOligosaccharidesPeptidoglycanPeptidoglycan Glycosyltransferase

Identifiers

PMID24255971
PMCPMC3944067
OpenAlexW2036613676

What OpenQuestion holds

Textmetadata
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.