Evidence map›Paper›PMID 28691491›Full record

ArticleJournal of the American Chemical Society2017

Peptidoglycan Cross-Linking Preferences of Staphylococcus aureus Penicillin-Binding Proteins Have Implications for Treating MRSA Infections.

Veerasak Srisuknimit, Yuan Qiao, Kaitlin Schaefer, Daniel Kahne, Suzanne Walker

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 72 citations in OpenAlex.

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  7. Control of morphogenesis during theScience advances · 2025
    Article
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  11. Sensitive and Extraction-Free Detection of Methicillin-ResistantJournal of microbiology and biotechnology · 2024
    Article
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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.

Veerasak SrisuknimitDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.
Yuan QiaoDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.
Kaitlin SchaeferDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.
Daniel KahneDepartment of Chemistry and Chemical Biology, Harvard University , Cambridge, Massachusetts 02138, United States.ORCID 0000-0002-8296-1424
Suzanne WalkerDepartment of Microbiology and Immunology, Harvard Medical School , Boston, Massachusetts 02138, United States.ORCID 0000-0002-0545-914X
Harvard University · US

Funding

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
NIGMS NIH HHS R01 GM066174NIGMS NIH HHS R01 GM076710
6 · The paper itself

Abstract

Methicillin-resistant Staphylococcus aureus (MRSA) infections are a global public health problem. MRSA strains have acquired a non-native penicillin-binding protein called PBP2a that cross-links peptidoglycan when the native S. aureus PBPs are inhibited by β-lactams. It has been proposed that the native S. aureus PBPs can use cell wall precursors having different glycine branch lengths (penta-, tri-, or monoglycine), while PBP2a can only cross-link peptidoglycan strands bearing a complete pentaglycine branch. This hypothesis has never been tested because the necessary substrates have not been available. Here, we compared the ability of PBP2a and two native S. aureus transpeptidases to cross-link peptidoglycan strands bearing different glycine branches. We show that purified PBP2a can cross-link glycan strands bearing penta- and triglycine, but not monoglycine, and experiments in cells provide support for these findings. Because PBP2a cannot cross-link peptidoglycan containing monoglycine, this study implicates the enzyme (FemA) that extends the monoglycine branch to triglycine on Lipid II as an ideal target for small molecules that restore sensitivity of MRSA to β-lactams.

Indexed as

Anti-Bacterial Agentsbeta-LactamsCross-Linking ReagentsMethicillin-Resistant Staphylococcus aureusMolecular StructurePenicillin-Binding ProteinsPeptidoglycanPeptidyl TransferasesStaphylococcal InfectionsAnti-Bacterial Agentsbeta-LactamsCross-Linking ReagentsPenicillin-Binding ProteinsPeptidoglycanPeptidyl Transferases

Identifiers

PMID28691491
PMCPMC5613940
OpenAlexW2735936858

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.