Evidence map›Paper›PMID 28166208›Full record

ArticleNature chemical biology2017

In vitro reconstitution demonstrates the cell wall ligase activity of LCP proteins.

Kaitlin Schaefer, Leigh M Matano, Yuan Qiao, Daniel Kahne, Suzanne Walker

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

54 citing papers in PubMed, 80 citations in OpenAlex.

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  9. SpbR controls lipoteichoic acid length by directly inhibiting signal peptidase SpsB inProceedings of the National Academy of Sciences of the United States of America · 2025
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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

5 authors at 1 institution in 1 country.

Kaitlin SchaeferDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, USA.
Leigh M MatanoDepartment of Microbiology and Immunology, Harvard Medical School, Boston, Massachusetts, USA.
Yuan QiaoDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, USA.
Daniel KahneDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, USA.
Suzanne WalkerDepartment of Microbiology and Immunology, Harvard Medical School, Boston, Massachusetts, USA.
Harvard University · US

Funding

Technical Mother Machine CoreP01AI083214 · NIAID · SCHEPENS EYE RESEARCH INSTITUTE · PI Michael S Gilmore · 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
Identifying and validating new antibiotic targets in cell wall synthesis pathwaysR01AI099144 · NIAID · HARVARD MEDICAL SCHOOL · PI BERNHARDT, THOMAS G, WALKER, SUZANNE · 2012 to 2016
$4.3M
NIAID NIH HHS P01 AI083214NIAID NIH HHS R01 AI099144NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

Sacculus is a peptidoglycan (PG) matrix that protects bacteria from osmotic lysis. In Gram-positive organisms, the sacculus is densely functionalized with glycopolymers important for survival, but the way in which assembly occurs is not known. In Staphylococcus aureus, three LCP (LytR-CpsA-Psr) family members have been implicated in attaching the major glycopolymer wall teichoic acid (WTA) to PG, but ligase activity has not been demonstrated for these or any other LCP proteins. Using WTA and PG substrates produced chemoenzymatically, we show that all three proteins can transfer WTA precursors to nascent PGs, establishing that LCP proteins are PG-glycopolymer ligases. Although all S. aureus LCP proteins have the capacity to attach WTA to PG, we show that their cellular functions are not redundant. Strains lacking lcpA have phenotypes similar to those of WTA-null strains, indicating that this is the most important WTA ligase. This work provides a foundation for studying how LCP enzymes participate in cell wall assembly.

Indexed as

Bacterial ProteinsCell WallIn Vitro TechniquesLigasesMolecular StructurePeptidoglycanStaphylococcus aureusBacterial ProteinsLigasesPeptidoglycan

Identifiers

PMID28166208
PMCPMC5362317
OpenAlexW2587265764

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.