Evidence map›Paper›PMID 37308592›Full record

ArticleNature microbiology2023

Mechanism of D-alanine transfer to teichoic acids shows how bacteria acylate cell envelope polymers.

Bailey J Schultz, Eric D Snow, Suzanne Walker

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. D-alanine aminotransferase (Dat) promotesbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. ThemBio · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Chemical biology tools to probe bacterial glycans.Current opinion in chemical biology · 2024
    Review
  14. Article
  15. Review
  16. 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 1 institution in 1 country.

Bailey J SchultzDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Eric D SnowDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
Suzanne WalkerDepartment of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA. suzanne_walker@hms.harvard.edu.ORCID http://orcid.org/0000-0002-0545-914X
Harvard University · US

Funding

Technical Mother Machine CoreP01AI083214 · NIAID · SCHEPENS EYE RESEARCH INSTITUTE · PI David C Hooper · 2009 to 2026
$39.4M
Project 3: Defining and defeating the mechanisms of outer membrane biogenesis in Gram-negative bacteriaU19AI158028 · NIAID · HARVARD MEDICAL SCHOOL · PI WALKER, SUZANNE · 2022 to 2025
$10.1M
Principles of Scientific Citizenship: Ethics, Communication, and Leadership for ScientistsT32GM095450 · NIGMS · HARVARD UNIVERSITY · PI WALKER, SUZANNE · 2011 to 2020
$3.5M
Harvard Chemical Biology PhD ProgramT32GM139775 · NIGMS · HARVARD UNIVERSITY · PI Emily Patricia Balskus, PHILIP A COLE · 2022 to 2026
$2.6M
NIAID NIH HHS P01 AI083214NIAID NIH HHS U19 AI158028NIGMS NIH HHS T32 GM095450NIGMS NIH HHS T32 GM139775
6 · The paper itself

Abstract

Bacterial cell envelope polymers are often modified with acyl esters that modulate physiology, enhance pathogenesis and provide antibiotic resistance. Here, using the D-alanylation of lipoteichoic acid (Dlt) pathway as a paradigm, we have identified a widespread strategy for how acylation of cell envelope polymers occurs. In this strategy, a membrane-bound O-acyltransferase (MBOAT) protein transfers an acyl group from an intracellular thioester onto the tyrosine of an extracytoplasmic C-terminal hexapeptide motif. This motif shuttles the acyl group to a serine on a separate transferase that moves the cargo to its destination. In the Dlt pathway, here studied in Staphylococcus aureus and Streptococcus thermophilus, the C-terminal 'acyl shuttle' motif that forms the crucial pathway intermediate is found on a transmembrane microprotein that holds the MBOAT protein and the other transferase together in a complex. In other systems, found in both Gram-negative and Gram-positive bacteria as well as some archaea, the motif is fused to the MBOAT protein, which interacts directly with the other transferase. The conserved chemistry uncovered here is widely used for acylation throughout the prokaryotic world.

Indexed as

Bacterial ProteinsPolymersAlanineBacteriaMicropeptidesTeichoic AcidsTransferasesAlanineBacterial ProteinsMicropeptidesPolymersTeichoic AcidsTransferases

Identifiers

PMID37308592
PMCPMC10664464
OpenAlexW4380319165

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.