Evidence map›Paper›PMID 27447281›Full record

ArticleMicrobial drug resistance (Larchmont, N.Y.)2016

Role of the N-Acetylmuramoyl-l-Alanyl Amidase, AmiA, of Helicobacter pylori in Peptidoglycan Metabolism, Daughter Cell Separation, and Virulence.

Catherine Chaput, Chantal Ecobichon, Nadine Pouradier, Jean-Claude Rousselle, Abdelkader Namane, Ivo G Boneca

Abstract read
In one paragraph

Article in Microbial drug resistance (Larchmont, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Pathogenicity ofWorld journal of clinical oncology · 2025
    Review
  2. Modelling host-pathogen interactions:Microbiology (Reading, England) · 2025
    Article
  3. Article
  4. Molecular Mechanisms of Biofilm Formation inAntibiotics (Basel, Switzerland) · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Interplay between Peptidoglycan Biology and Virulence in Gram-Negative Pathogens.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  14. Morphology ofPrzeglad gastroenterologiczny · 2018
    Review
  15. Review
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

6 authors.

Catherine Chaput1 Institut Pasteur, Unite de Pathogénie Bactérienne des Muqueuses , Paris, France .
Chantal Ecobichon1 Institut Pasteur, Unite de Pathogénie Bactérienne des Muqueuses , Paris, France .
Nadine Pouradier1 Institut Pasteur, Unite de Pathogénie Bactérienne des Muqueuses , Paris, France .
Jean-Claude Rousselle4 Institut Pasteur, Plate-forme de Protéomique, Paris, France .
Abdelkader Namane4 Institut Pasteur, Plate-forme de Protéomique, Paris, France .
Ivo G Boneca1 Institut Pasteur, Unite de Pathogénie Bactérienne des Muqueuses , Paris, France .

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human gastric pathogen, Helicobacter pylori, is becoming increasingly resistant to most available antibiotics. Peptidoglycan (PG) metabolism is essential to eubacteria, hence, an excellent target for the development of new therapeutic strategies. However, our knowledge on PG metabolism in H. pylori remains poor. We have further characterized an isogenic mutant of the amiA gene encoding a N-acetylmuramoyl-l-alanyl amidase. The amiA mutant displayed long chains of unseparated cells, an impaired motility despite the presence of intact flagella and a tolerance to amoxicillin. Interestingly, the amiA mutant was impaired in colonizing the mouse stomach suggesting that AmiA is a valid target in H. pylori for the development of new antibiotics. Using reverse phase high-pressure liquid chromatography, we analyzed the PG muropeptide composition and glycan chain length distribution of strain 26695 and its amiA mutant. The analysis showed that H. pylori lacked muropeptides with a degree of cross-linking higher than dimeric muropeptides. The amiA mutant was also characterized by a decrease of muropeptides carrying 1,6-anhydro-N-acetylmuramic acid residues, which represent the ends of the glycan chains. This correlated with an increase of very long glycan strands in the amiA mutant. It is suggested that these longer glycan strands are trademarks of the division site. Taken together, we show that the low redundancy on genes involved in PG maturation supports H. pylori as an actractive alternative model to study PG metabolism and cell shape regulation.

Indexed as

AmidohydrolasesAmoxicillinAnimalsAnti-Bacterial AgentsBacterial ProteinsCell DivisionGene ExpressionHelicobacter InfectionsHelicobacter pyloriMiceMice, Inbred C57BLMuramic AcidsMutationPeptidoglycanStomachVirulenceAmidohydrolasesAmoxicillinanhydro-N-acetylmuramic acidAnti-Bacterial AgentsBacterial ProteinsMuramic AcidsPeptidoglycan

Identifiers

PMID27447281
PMCPMC5036311

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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.