Evidence map›Paper›PMID 20368342›Full record

ArticleInfection and immunity2010

Coupled amino acid deamidase-transport systems essential for Helicobacter pylori colonization.

Damien Leduc, Julien Gallaud, Kerstin Stingl, Hilde de Reuse

Abstract read
In one paragraph

Article in Infection and immunity, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

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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

4 authors.

Damien LeducDépartement de Microbiologie, Unité Pathogenèse de Helicobacter, Institut Pasteur, 28 rue du Dr Roux, 75724 Paris cedex 15, France.
Julien Gallaud
Kerstin Stingl
Hilde de Reuse

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to their classical roles as carbon or nitrogen sources, amino acids can be used for bacterial virulence, colonization, or stress resistance. We found that original deamidase-transport systems impact colonization by Helicobacter pylori, a human pathogen associated with gastric pathologies, including adenocarcinoma. We demonstrated that l-asparaginase (Hp-AnsB) and gamma-glutamyltranspeptidase (Hp-gammaGT) are highly active periplasmic deamidases in H. pylori, producing ammonia and aspartate or glutamate from asparagine and glutamine, respectively. Hp-GltS was identified as a sole and specialized transporter for glutamate, while aspartate was exclusively imported by Hp-DcuA. Uptake of Gln and Asn strictly relies on indirect pathways following prior periplasmic deamidation into Glu and Asp. Hence, in H. pylori, the coupled action of periplasmic deamidases with their respective transporters enables the acquisition of Glu and Asp from Gln and Asn, respectively. These systems were active at neutral rather than acidic pH, suggesting their function near the host epithelial cells. We showed that Hp-DcuA, the fourth component of these novel deamidase-transport systems, was as crucial as Hp-gammaGT, Hp-AnsB, and Hp-GltS for animal model colonization. In conclusion, the pH-regulated coupled amino acid deamidase-uptake system represents an original optimized system that is essential for in vivo colonization of the stomach environment by H. pylori. We propose a model in which these two nonredundant systems participate in H. pylori virulence by depleting gastric or immune cells from protective amino acids such as Gln and producing toxic ammonia close to the host cells.

Indexed as

Amino AcidsAmino Acid Transport Systems, AcidicAmmoniaAnimalsAsparaginaseAspartic AcidBacterial ProteinsColony Count, MicrobialDicarboxylic Acid Transportersgamma-GlutamyltransferaseGlutamic AcidHelicobacter pyloriHumansHydrogen-Ion ConcentrationMiceModels, BiologicalAmino AcidsAmino Acid Transport Systems, AcidicAmmoniaAsparaginaseAspartic AcidBacterial ProteinsDcuA dicarboxylate transporter, bacteriaDicarboxylic Acid Transportersgamma-GlutamyltransferaseGlutamic AcidVirulence Factors

Identifiers

PMID20368342
PMCPMC2876568

What OpenQuestion holds

Textmetadata
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.