Evidence map›Paper›PMID 24733938›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Lipopolysaccharide O antigen size distribution is determined by a chain extension complex of variable stoichiometry in Escherichia coli O9a.

Jerry D King, Scott Berry, Bradley R Clarke, Richard J Morris, Chris Whitfield

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Identification of a second glycoform of the clinically prevalent O1 antigen fromProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Cryo-EM structure of the full-length WzmWzt ABC transporter required for lipid-linked O antigen transport.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  10. Review
  11. Article
  12. Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020
    Review
  13. An Evolutionary Arms Race BetweenFrontiers in microbiology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Single polysaccharide assembly protein that integrates polymerization, termination, and chain-length quality control.Proceedings of the National Academy of Sciences of the United States of America · 2017
    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

5 authors.

Jerry D KingMolecular and Cellular Biology, University of Guelph, Guelph, ON, Canada N1G 2W1.
Scott Berry
Bradley R Clarke
Richard J Morris
Chris Whitfield

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/000C0640
6 · The paper itself

Abstract

The lengths of bacterial polysaccharides can be critical for their biological function. Unlike DNA or protein synthesis, where polymer length is implicit in the nucleic acid template, the molecular mechanisms for regulating polysaccharide length are poorly understood. Two models are commonly cited: a "molecular clock" regulates length by controlling the duration of the polymer extension process, whereas a "molecular ruler" determines length by measurement against a physical structure in the biosynthetic complex. Escherichia coli O9a is a prototype for the biosynthesis of O polysaccharides by ATP-binding cassette transporter-dependent processes. The length of the O9a polysaccharide is determined by two proteins: an extension enzyme, WbdA, and a termination enzyme, WbdD. WbdD is known to self-oligomerize and also to interact with WbdA. Changing either enzyme's concentration can alter the polysaccharide length. We quantified the O9a polysaccharide length distribution and the enzyme concentration dependence in vivo, then made mathematical models to predict the polymer length distributions resulting from hypothetical length-regulation mechanisms. Our data show qualitative features that cannot be explained by either a molecular clock or a molecular ruler model. Therefore, we propose a "variable geometry" model, in which a postulated biosynthetic WbdA-WbdD complex assembles with variable stoichiometry dependent on relative enzyme concentration. Each stoichiometry produces polymers with a distinct, geometrically determined, modal length. This model reproduces the enzyme concentration dependence and modality of the observed polysaccharide length distributions. Our work highlights limitations of previous models and provides new insight into the mechanisms of length control in polysaccharide biosynthesis.

Indexed as

Escherichia coliEscherichia coli ProteinsMannosyltransferasesModels, BiologicalMolecular WeightO AntigensEscherichia coli ProteinsMannosyltransferasesO AntigensWbdA protein, E colichain lengthmathematical modelingtemplate-independent polymerization

Identifiers

PMID24733938
PMCPMC4035927

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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.