Evidence map›Paper›PMID 34168115›Full record

ReviewNutrition & diabetes2021

Amino acid metabolism and signalling pathways: potential targets in the control of infection and immunity.

Daniel Tomé

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Nutrition & diabetes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 67 citations in OpenAlex.

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  12. Circadian metabolic adaptations to infections.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

1 author at 1 institution in 1 country.

Daniel ToméUMR PNCA, AgroParisTech, INRAE, Université Paris-Saclay, Paris, France. tome.daniel@orange.fr.ORCID http://orcid.org/0000-0001-9604-5972
AgroParisTech · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Defences to pathogens such as SarCoV2 in mammals involves interactions between immune functions and metabolic pathways to eradicate infection while preventing hyperinflammation. Amino acid metabolic pathways represent with other antimicrobial agent potential targets for therapeutic strategies. iNOS-mediated production of NO from Arg is involved in the innate inflammatory response to pathogens and NO overproduction can induce hyperinflammation. The two Arg-catabolising enzymes Arg1 and IDO1 reduce the hyperinflammation by an immunosuppressive effect via either Arg starvation (for Arg1) or via the immunoregulatory activity of the Arg-derived metabolites Kyn (for IDO1). In response to amino acid abundance mTOR activates the host protein translation and Coronaviruses use this machinery for their own protein synthesis and replication. In contrast GCN2, the sensor of amino acid starvation, activates pathways that restrict inflammation and viral replication. Gln depletion alters the immune response that become more suppressive, by favouring a regulatory T phenotype rather than a Th1 phenotype. Proliferating activated immune cells are highly dependent on Ser, activation and differentiation of T cells need enough Ser and dietary Ser restriction can inhibit their proliferation. Cys is strictly required for T-cell proliferation because they cannot convert Met to Cys. Restricting Met inhibits both viral RNA cap methylation and replication, and the proliferation of infected cells with an increased requirement for Met. Phe catabolism produces antimicrobial metabolites resulting in the inhibition of microbial growth and an immunosuppressive activity towards T lymphocytes.

Indexed as

Immunity, InnateAmino AcidsAnimalsAnti-Infective AgentsArginineHumansInfectionsInflammationNitric Oxide Synthase Type IISignal TransductionT-LymphocytesTOR Serine-Threonine KinasesVirus ReplicationAmino AcidsAnti-Infective AgentsArginineMTOR protein, humanNitric Oxide Synthase Type IINOS2 protein, humanTOR Serine-Threonine Kinases

Identifiers

PMID34168115
PMCPMC8223530
OpenAlexW3173579810

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.