Evidence map›Paper›PMID 42497854›Full record

ArticleMolecular cell2026

The Legionella pneumophila effector SidL is an adenylyltransferase that modifies the glycolytic intermediate 3-phosphoglycerate.

Joshua J Black, A Maxwell Burroughs, Edrees H Rashan, Charles R Nosal, Katerina A Romanov, Marco A Catipovic, Catherine Valadez, L Aravind, Kevin G Hicks, Caren L Freel Meyers and 3 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular cell, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Joshua J BlackDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Howard Hughes Medical Institute, Chevy Chase, MD, USA.
A Maxwell BurroughsComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.
Edrees H RashanKoch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
Charles R NosalDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Chemistry-Biology Interface Graduate Training Program, Johns Hopkins University, Baltimore, MD, USA.
Katerina A RomanovDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Marco A CatipovicDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Howard Hughes Medical Institute, Chevy Chase, MD, USA.
Catherine ValadezDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
L AravindComputational Biology Branch, Division of Intramural Research, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA.
Kevin G HicksDepartment of Nutrition & Integrative Physiology, University of Utah College of Health, Salt Lake City, UT, USA.
Caren L Freel MeyersDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Chemistry-Biology Interface Graduate Training Program, Johns Hopkins University, Baltimore, MD, USA.
Tamara J O'ConnorDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Matthew G Vander HeidenKoch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA, USA; Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA; Dana-Farber Cancer Institute, Boston, MA, USA.
Rachel GreenDepartment of Molecular Biology & Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA; Howard Hughes Medical Institute, Chevy Chase, MD, USA. Electronic address: ragreen@jhmi.edu.

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MATTHEW G. VANDER HEIDEN · 1985 to 2026
$93.9M
Evolutionary Analysis and Comparative Genomics of Protein SuperfamiliesZIALM594244 · NLM · NATIONAL LIBRARY OF MEDICINE · PI ARAVIND, L · 2009 to 2025
$20.3M
Proteomics CoreU54DK110858 · NIDDK · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI Anna E Beaudin, JAMES Eric COX · 2016 to 2026
$8.6M
Understanding the role of metabolism in cancerR35CA242379 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI VANDER HEIDEN, MATTHEW G. · 2019 to 2025
$5.8M
Acquisition of a 500 MHz NMR Spectrometer to Support Small-Molecule Chemistry at Johns Hopkins Medical SchoolS10OD034217 · OD · JOHNS HOPKINS UNIVERSITY · PI BHAT, SHRIDHAR · 2024 to 2024
$425k
Characterizing host translation inhibition by Legionella pneumophilaF32AI181301 · NIAID · JOHNS HOPKINS UNIVERSITY · PI Joshua J Black · 2024 to 2026
$234k
Howard Hughes Medical InstituteIntramural NIH HHS ZIA LM594244NCI NIH HHS P30 CA014051NCI NIH HHS R35 CA242379NIAID NIH HHS F32 AI181301NIDDK NIH HHS U54 DK110858NIH HHS S10 OD034217
6 · The paper itself

Abstract

The large effector arsenal of the bacterial pathogen Legionella pneumophila has been a rich source of biochemistry, highlighting the immense diversity of strategies deployed in host-pathogen conflict. Here, we redefine the purported translation inhibitor SidL as an adenylyltransferase that targets a glycolytic metabolite, discovering that it modifies 3-phosphoglycerate with adenosine monophosphate (AMP) to produce the previously unknown molecule 2-AMP-3-phosphoglycerate. When expressed alone in mammalian cells, SidL adenylates 3-phosphoglycerate, disrupts glycolysis, and blocks the nutrient-responsive translation regulator mTORC1, which we propose indirectly causes translation inhibition. Moreover, we observe SidL-dependent production of 2-AMP-3-phosphoglycerate in macrophages during L. pneumophila infection, the timing of which is consistent with a role for SidL in the early stages of the infection cycle. Thus, our study uncovers a mechanism by which an intracellular pathogen uses the chemical modification of a glycolytic intermediate to target central carbon metabolism in the host.

Indexed as

Bacterial ProteinsGlyceric AcidsGlycolysisLegionella pneumophilaLegionnaires' DiseaseNucleotidyltransferasesAdenosine MonophosphateAnimalsHEK293 CellsHost-Pathogen InteractionsHumansMacrophagesMechanistic Target of Rapamycin Complex 1Mice3-phosphoglycerateAdenosine MonophosphateBacterial ProteinsGlyceric AcidsMechanistic Target of Rapamycin Complex 1Nucleotidyltransferases3-phosphoglycerateAdenylyltransferaseAMPAMPylasebacterial pathogenesisCeg14glycolysisLegionella pneumophilaLpg0437MCF1-SHEmTORPAP2SidLSidL/Ceg14/Lpg0437

Identifiers

PMID42497854
PMCPMC13431035

What OpenQuestion holds

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Registered trials

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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.